메뉴 건너뛰기




Volumn 16, Issue 4, 1983, Pages 521-655

Hydrogen exchange and structural dynamics of proteins and nucleic acids

Author keywords

[No Author keywords available]

Indexed keywords

APROTININ; DNA; PROTEIN; RIBONUCLEASE; RIBONUCLEASE S; RNA; SOLVENT;

EID: 0020855355     PISSN: 00335835     EISSN: 14698994     Source Type: Journal    
DOI: 10.1017/S0033583500005217     Document Type: Article
Times cited : (1292)

References (244)
  • 1
    • 0020793447 scopus 로고
    • Hydrogen exchange studies of proteins: recent advances in medium and high resolution methods
    • ALLEWELL, N. M. (1983). Hydrogen exchange studies of proteins: recent advances in medium and high resolution methods. J. Biochem. Biophys. Methods. 7, 345-357.
    • (1983) J. Biochem. Biophys. Methods. , vol.7 , pp. 345-357
    • ALLEWELL, N.M.1
  • 2
    • 0015852595 scopus 로고
    • Nucleic acid-solvent interactions: temperature dependence of the heat of solution of thymine in water and ethanol
    • ALVAREZ, J. & BILTONEN, R. L. (1973). Nucleic acid-solvent interactions: temperature dependence of the heat of solution of thymine in water and ethanol. Biopolymers 12, 1815–1828.
    • (1973) Biopolymers , vol.12 , pp. 1815-1828
    • ALVAREZ, J.1    BILTONEN, R.L.2
  • 3
    • 84984088084 scopus 로고
    • Hydroxamate complexes.
    • Fe(m) exchange between sideramines and complexons. Discussion of the binding constants of hydroxamate complexes.
    • ANDEREGG, G., L’EPLATTENIER, F. & SCHWARZENBACH, G. (1963). Hydroxamate complexes. III. Fe(m) exchange between sideramines and complexons. Discussion of the binding constants of hydroxamate complexes. Helv. chim. Acta 46, 1409—1422.
    • (1963) Helv. chim. Acta , vol.46 , Issue.3 , pp. 1409-1422
    • ANDEREGG, G.1    L’EPLATTENIER, F.2    SCHWARZENBACH, G.3
  • 5
    • 0020789053 scopus 로고
    • efferent of the presence of water on lysozyme conformation.
    • BAKER, L. J., HANSEN, A. M. F., RAO, P. B. & BRYAN, W. P. (1983). efferent of the presence of water on lysozyme conformation. Biopolymers 22, 1637–1640.
    • (1983) Biopolymers , vol.22 , pp. 1637-1640
    • BAKER, L.J.1    HANSEN, A.M.F.2    RAO, P.B.3    BRYAN, W.P.4
  • 6
    • 0016418420 scopus 로고
    • Intermediates in protein folding reactions and the mechanism of protein unfolding
    • BALDWIN, R. L. (1975). Intermediates in protein folding reactions and the mechanism of protein unfolding. A. Rev. Biochem. 44, 453–475.
    • (1975) A. Rev. Biochem. , vol.44 , pp. 453-475
    • BALDWIN, R.L.1
  • 7
    • 0007291003 scopus 로고
    • Recent experimental work on the pathway and mechanism of protein folding.
    • (ed. R. Jaenicke), Amsterdam: Elsevier-North Holland
    • BALDWIN, R. L. & CREIGHTON, T. E. (1980). Recent experimental work on the pathway and mechanism of protein folding. In Protein Folding (ed. R. Jaenicke), pp. 217–259. Amsterdam: Elsevier-North Holland.
    • (1980) Protein Folding , pp. 217-259
    • BALDWIN, R.L.1    CREIGHTON, T.E.2
  • 8
    • 36749121933 scopus 로고
    • Theory of twisting and bending of chain macromolecules: analysis of the fluorescence depolarization of DNA.
    • BARKLEY, M. D. & ZIMM, B. H. (1979). Theory of twisting and bending of chain macromolecules: analysis of the fluorescence depolarization of DNA. J. chem. Phys. 70, 2991–3007.
    • (1979) J. chem. Phys. , vol.70 , pp. 2991-3007
    • BARKLEY, M.D.1    ZIMM, B.H.2
  • 9
    • 0003772576 scopus 로고
    • Determination of pH: Theory and Practice
    • 2nd ed. New York: Wiley
    • BATES, R. G. (1964). Determination of pH: Theory and Practice, 2nd ed. New York: Wiley.
    • (1964)
    • BATES, R.G.1
  • 12
    • 0001121381 scopus 로고
    • Deuterium exchange of poly-DL-alanine in aqueous solution.
    • BERGER, A. & LINDERSTROM-LANG, K. (1957). Deuterium exchange of poly-DL-alanine in aqueous solution. Archs Biochem. Biophys. 69, 106–118.
    • (1957) Archs Biochem. Biophys. , vol.69 , pp. 106-118
    • BERGER, A.1    LINDERSTROM-LANG, K.2
  • 13
    • 0001347959 scopus 로고
    • A nuclear magnetic resonance study of the protolysis and ionization of A/-methylacetamide.
    • BERGER, A., LOEWENSTEIN, A. & MEIBOOM, S. (1959). A nuclear magnetic resonance study of the protolysis and ionization of A/-methylacetamide. J. Am. chem. Soc. 81, 62–67.
    • (1959) J. Am. chem. Soc. , vol.81 , pp. 62-67
    • BERGER, A.1    LOEWENSTEIN, A.2    MEIBOOM, S.3
  • 14
    • 0021095481 scopus 로고
    • X-ray studies of water in crystals of lysozyme.
    • BLAKE, C. C. F., PULFORD, W. C. A. & ARTYMIUK, P. J. (1983) X-ray studies of water in crystals of lysozyme. J. molec. Biol. 167, 693–723.
    • (1983) J. molec. Biol. , vol.167 , pp. 693-723
    • BLAKE, C.C.F.1    PULFORD, W.C.A.2    ARTYMIUK, P.J.3
  • 15
    • 9244238010 scopus 로고
    • Fast and slow conformational fluctuations of RNA and DNA.
    • Subnanosecond internal motion correlation times determined by 31P NMR.
    • BOLTON, P. H. & JAMES, T. L. (1980). Fast and slow conformational fluctuations of RNA and DNA. Subnanosecond internal motion correlation times determined by 31P NMR. J. Am. chem. Soc. 102, 25 – 313
    • (1980) J. Am. chem. Soc. , vol.102 , pp. 25-313
    • BOLTON, P.H.1    JAMES, T.L.2
  • 16
    • 84985644090 scopus 로고
    • Dependence of DNA conformation on the concentration of salt.
    • BOROCHOV, N., EISENBERG, H. & KAM, Z. (1981). Dependence of DNA conformation on the concentration of salt. Biopolymers 20, 231–235.
    • (1981) Biopolymers , vol.20 , pp. 231-235
    • BOROCHOV, N.1    EISENBERG, H.2    KAM, Z.3
  • 17
    • 0001030217 scopus 로고
    • Conformation of cyclolinopeptide A observed by NMR spectroscopy
    • BREWSTER, A. I. & BOVEY, F. A. (1971). Conformation of cyclolinopeptide A observed by NMR spectroscopy. Proc. natn. Acad. Sci. U.S.A. 68, 1199–1202.
    • (1971) Proc. natn. Acad. Sci. U.S.A. , vol.68 , pp. 1199-1202
    • BREWSTER, A.I.1    BOVEY, F.A.2
  • 18
    • 0017848335 scopus 로고
    • nuclear magnetic resonance studies of the native and the transaminated inhibitor.
    • The influence of a single salt bridge on static and dynamic features of the globular solution conformation of the basic pancreatic trypsin inhibitor. ‘14 and 13C
    • BROWN, L. R., DEMARCO, A., RICHARZ, R., WAGNER, G. & WUTHRICH, K. (1978). The influence of a single salt bridge on static and dynamic features of the globular solution conformation of the basic pancreatic trypsin inhibitor. ‘14 and 13C nuclear magnetic resonance studies of the native and the transaminated inhibitor. Eur. J. Biochem. 88, 87–95.
    • (1978) Eur. J. Biochem. , vol.88 , pp. 87-95
    • BROWN, L.R.1    DEMARCO, A.2    RICHARZ, R.3    WAGNER, G.4    WUTHRICH, K.5
  • 19
    • 0012150983 scopus 로고
    • The mechanism of hydrogen exchange in proteins
    • BRYAN, W. D. (1970). The mechanism of hydrogen exchange in proteins. Recent Prog. Surf Sci. 3, 101–120.
    • (1970) Recent Prog. Surf Sci. , vol.3 , pp. 101-120
    • BRYAN, W.D.1
  • 20
    • 0019072889 scopus 로고
    • Dynamical deductions from NMR relaxation measurements at the water-protein interface
    • BRYANT, R. G. & SHIPLEY, W. M. (1980). Dynamical deductions from NMR relaxation measurements at the water-protein interface. Biophys. J. 32, 3–11.
    • (1980) Biophys. J. , vol.32 , pp. 3-11
    • BRYANT, R.G.1    SHIPLEY, W.M.2
  • 21
    • 0021114740 scopus 로고
    • Penetration of small molecules into proteins studied by quenching of phosphorescence and fluorescence
    • CALHOUN, D. B., VANDERKOOI, J. M. & ENGLANDER, S. W. (1983). Penetration of small molecules into proteins studied by quenching of phosphorescence and fluorescence. Biochemistry 22, 1533–1539.
    • (1983) Biochemistry , vol.22 , pp. 1533-1539
    • CALHOUN, D.B.1    VANDERKOOI, J.M.2    ENGLANDER, S.W.3
  • 22
    • 0021114712 scopus 로고
    • Penetration of dioxygen into proteins studied by quenching of phosphorescence and fluorescence.
    • CALHOUN, D. B., VANDERKOOI, J. M., WOODROW III, G. W. & ENGLANDER, S. W. (1983). Penetration of dioxygen into proteins studied by quenching of phosphorescence and fluorescence. Biochemistry 22, 1526–1532.
    • (1983) Biochemistry , vol.22 , pp. 1526-1532
    • CALHOUN, D.B.1    VANDERKOOI, J.M.2    WOODROW, G.W.3    ENGLANDER, S.W.4
  • 24
    • 0017801999 scopus 로고
    • Pressure effects on folded proteins in solution.
    • CARTER, J. V., KNOX, D. G. & ROSENBERG, A. (1978). Pressure effects on folded proteins in solution. J. biol. Chem. 253, 1947–1953.
    • (1978) J. biol. Chem. , vol.253 , pp. 1947-1953
    • CARTER, J.V.1    KNOX, D.G.2    ROSENBERG, A.3
  • 25
    • 0018791973 scopus 로고
    • Dynamics of ligand binding to heme proteins
    • CASE, D. A. & KARPLUS, M. (1979). Dynamics of ligand binding to heme proteins. J. molec. Biol. 132, 343–368.
    • (1979) J. molec. Biol. , vol.132 , pp. 343-368
    • CASE, D.A.1    KARPLUS, M.2
  • 26
    • 0017187836 scopus 로고
    • The nature of the accessible and buried surfaces in proteins.
    • CHOTHIA, C. (1976). The nature of the accessible and buried surfaces in proteins. J. molec. Biol. 105, 1–14.
    • (1976) J. molec. Biol. , vol.105 , pp. 1-14
    • CHOTHIA, C.1
  • 27
    • 0343063933 scopus 로고
    • Structure of proteins: packing of alpha-helices and pleated sheets.
    • CHOTHIA, C. LEVITT, M. & RICHARDSON, D. (1977). Structure of proteins: packing of alpha-helices and pleated sheets. Proc. natn. Acad. Sci. U.S.A. 74, 4130–4134.
    • (1977) Proc. natn. Acad. Sci. U.S.A. , vol.74 , pp. 4130-4134
    • CHOTHIA, C.1    LEVITT, M.2    RICHARDSON, D.3
  • 28
    • 84976073388 scopus 로고
    • Molecular surfaces and interior cavities of proteins
    • CONNOLLY, M. L. (1981). Molecular surfaces and interior cavities of proteins. Ph.D. dissertation UCSF.
    • (1981) Ph.D. dissertation UCSF
    • CONNOLLY, M.L.1
  • 29
    • 0000725483 scopus 로고
    • Thermodynamic fluctuations in protein molecules
    • COOPER, A. (1976). Thermodynamic fluctuations in protein molecules. Proc. natn. Acad. Sci. U.S.A. 73, 2740–2741.
    • (1976) Proc. natn. Acad. Sci. U.S.A. , vol.73 , pp. 2740-2741
    • COOPER, A.1
  • 30
    • 0017815610 scopus 로고
    • Experimental studies of protein folding and unfolding
    • CREIGHTON, T. E. (1979). Experimental studies of protein folding and unfolding. Prog. Biophys. molec. Biol. 33, 231–297.
    • (1979) Prog. Biophys. molec. Biol. , vol.33 , pp. 231-297
    • CREIGHTON, T.E.1
  • 31
    • 0016441208 scopus 로고
    • Hydrogen exchange in nucleosides and nucleotides
    • Measurement of hydrogen exchange by stopped-flow and ultraviolet difference spectroscopy
    • CROSS, D. G. (1975). Hydrogen exchange in nucleosides and nucleotides. Measurement of hydrogen exchange by stopped-flow and ultraviolet difference spectroscopy. Biochemistry 14, 357–362.
    • (1975) Biochemistry , vol.14 , pp. 357-362
    • CROSS, D.G.1
  • 32
    • 0016169138 scopus 로고
    • The molecular mechanism of thermal unfolding of Escherichia-Coli formyl methionine transfer RNA
    • CROTHERS, D. M., COLE, P. E., HILBERS, C. W. & SHULMAN, R. G. (1974). The molecular mechanism of thermal unfolding of Escherichia-Coli formyl methionine transfer RNA. J. molec. Biol. 87, 63–88.
    • (1974) J. molec. Biol. , vol.87 , pp. 63-88
    • CROTHERS, D.M.1    COLE, P.E.2    HILBERS, C.W.3    SHULMAN, R.G.4
  • 33
    • 0001434099 scopus 로고
    • Proton NMR study of the relaxation behavior and kinetic lability of exchangeable protons in the heme pocket of cyanomet myoglobin.
    • CUTNELL, J. D., LAMAR, G. N. & KONG, S. B. (1981). Proton NMR study of the relaxation behavior and kinetic lability of exchangeable protons in the heme pocket of cyanomet myoglobin. J. Am. chem. Soc. 103, 3567–3582.
    • (1981) J. Am. chem. Soc. , vol.103 , pp. 3567-3582
    • CUTNELL, J.D.1    LAMAR, G.N.2    KONG, S.B.3
  • 34
    • 0001612915 scopus 로고
    • Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at 1’5 A resolution
    • DEISENHOFER, J. & STEIGEMANN, W. (1975). Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at 1’5 A resolution. Acta crystallogr B 31, 238–250.
    • (1975) Acta crystallogr B , vol.31 , pp. 238-250
    • DEISENHOFER, J.1    STEIGEMANN, W.2
  • 35
    • 49149143351 scopus 로고
    • Solvent effects and approaches for the fine structure analysis of peptidyl amide 1H NMR spectra.
    • DEMARCO, A. & LUNAS, M. (1980). Solvent effects and approaches for the fine structure analysis of peptidyl amide 1H NMR spectra. J. magn. Reson. 39, 253–262.
    • (1980) J. magn. Reson. , vol.39 , pp. 253-262
    • DEMARCO, A.1    LUNAS, M.2
  • 36
    • 0018802422 scopus 로고
    • Individual assignments of amide proton resonances in the proton NMR spectrum of the basic pancreatic trypsin inhibitor.
    • DUBS, A., WAGNER, G. & WUTHRICH, K. (1979). Individual assignments of amide proton resonances in the proton NMR spectrum of the basic pancreatic trypsin inhibitor. Biochim. biophys. Acta 577, 177–194.
    • (1979) Biochim. biophys. Acta , vol.577 , pp. 177-194
    • DUBS, A.1    WAGNER, G.2    WUTHRICH, K.3
  • 37
    • 0019886913 scopus 로고
    • A 300 megahertz proton NMR investigation of DNA restriction fragments dynamic properties.
    • EARLY, T. A., KEARNS, D. R., HILLEN, W. & WELLS, R. D. (1981). A 300 megahertz proton NMR investigation of DNA restriction fragments dynamic properties. Biochemistry 20, 3764–3769.
    • (1981) Biochemistry , vol.20 , pp. 3764-3769
    • EARLY, T.A.1    KEARNS, D.R.2    HILLEN, W.3    WELLS, R.D.4
  • 38
    • 0000767837 scopus 로고
    • Dynamics of a protein matrix revealed by flourescence quenching
    • EFTINK, M. R. & GHIRON, C. A. (1975). Dynamics of a protein matrix revealed by flourescence quenching. Proc. natn. Acad. Sci. U.S.A. 72, 3290–3294.
    • (1975) Proc. natn. Acad. Sci. U.S.A. , vol.72 , pp. 3290-3294
    • EFTINK, M.R.1    GHIRON, C.A.2
  • 39
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • EFTINK, M. R. & GHIRON, C. A. (1981). Fluorescence quenching studies with proteins. Analyt. Biochem. 114, 199–227.
    • (1981) Analyt. Biochem. , vol.114 , pp. 199-227
    • EFTINK, M.R.1    GHIRON, C.A.2
  • 40
    • 0001957353 scopus 로고
    • Proton transfer, acid-base catalysis, and enzymatic hydrolysis.
    • EIGEN, M. (1964). Proton transfer, acid-base catalysis, and enzymatic hydrolysis. Angew. Chem. Ed. 3, 1–19.
    • (1964) Angew. Chem. Ed. , vol.3 , pp. 1-19
    • EIGEN, M.1
  • 41
    • 0016762137 scopus 로고
    • Hydrogen-tritium exchange kinetics of soybean trypsin inhibitor
    • Solvent accessibility in the folded conformation
    • ELLIS, L. M., BLOOMFIELD, V. A. & WOODWARD, C. K. (1975). Hydrogen-tritium exchange kinetics of soybean trypsin inhibitor. Solvent accessibility in the folded conformation. Biochemistry 14, 3413–3419.
    • (1975) Biochemistry , vol.14 , pp. 3413-3419
    • ELLIS, L.M.1    BLOOMFIELD, V.A.2    WOODWARD, C.K.3
  • 42
    • 0014174696 scopus 로고
    • Slow tritium-hydrogen exchange in some peptide chelates
    • EMERY, T. F. (1967). Slow tritium-hydrogen exchange in some peptide chelates. Biochemistry 6, 3858–3866.
    • (1967) Biochemistry , vol.6 , pp. 3858-3866
    • EMERY, T.F.1
  • 43
    • 0018790558 scopus 로고
    • Measurement and calibration of peptide group hydrogen-deuterium exchange by ultraviolet spectrophotometry
    • ENGLANDER, J. J., CALHOUN, D. B. & ENGLANDER, S. W. (1979). Measurement and calibration of peptide group hydrogen-deuterium exchange by ultraviolet spectrophotometry. Analyt. Biochem. 92, 517–524.
    • (1979) Analyt. Biochem. , vol.92 , pp. 517-524
    • ENGLANDER, J.J.1    CALHOUN, D.B.2    ENGLANDER, S.W.3
  • 44
    • 0020490880 scopus 로고
    • Reexamination of rhodopsin structure by hydrogen exchange.
    • ENGLANDER, J. J., DOWNER, N. W. & ENGLANDER, S. W. (1982). Reexamination of rhodopsin structure by hydrogen exchange. J. biol. Chem. y257, 7982–7986.
    • (1982) J. biol. Chem. , vol.y257 , pp. 7982-7986
    • ENGLANDER, J.J.1    DOWNER, N.W.2    ENGLANDER, S.W.3
  • 46
    • 0015505353 scopus 로고
    • Hydrogen exchange study of some polynucleotides and transfer RNA
    • ENGLANDER, J. J., KALLENBACH, N. R. & ENGLANDER, S. W. (1972). Hydrogen exchange study of some polynucleotides and transfer RNA. J. molec. Biol. 63, 153–169.
    • (1972) J. molec. Biol. , vol.63 , pp. 153-169
    • ENGLANDER, J.J.1    KALLENBACH, N.R.2    ENGLANDER, S.W.3
  • 47
    • 0020607281 scopus 로고
    • Identification of an allosterically sensitive unfolding unit in hemoglobin.
    • ENGLANDER, J. J., ROGERO, J. R. & ENGLANDER, S. W. (1983). Identification of an allosterically sensitive unfolding unit in hemoglobin. J. molec. Biol. 169, 325 – 344.
    • (1983) J. molec. Biol. , vol.169 , pp. 325-344
    • ENGLANDER, J.J.1    ROGERO, J.R.2    ENGLANDER, S.W.3
  • 48
    • 0016591714 scopus 로고
    • Measurement of structural and free energy changes in hemoglobin by hydrogen exchange methods
    • ENGLANDER, S. W. (1975). Measurement of structural and free energy changes in hemoglobin by hydrogen exchange methods. Ann. N. Y. Acad. Sci. 244, 10–27.
    • (1975) Ann. N. Y. Acad. Sci. , vol.244 , pp. 10-27
    • ENGLANDER, S.W.1
  • 51
    • 84908749127 scopus 로고
    • Functional labelling of proteins in hemoglobin.
    • ed. E. Clementi and R. H. Sarma, New York: Adenine Press
    • ENGLANDER, S. W. & ENGLANDER, J. J. (1983). Functional labelling of proteins in hemoglobin. In Structure and Dynamics of Nucleic Acids and Proteins (ed. E. Clementi and R. H. Sarma), pp. 421–433. New York: Adenine Press.
    • (1983) Structure and Dynamics of Nucleic Acids and Proteins , pp. 421-433
    • ENGLANDER, S.W.1    ENGLANDER, J.J.2
  • 53
    • 0015522897 scopus 로고
    • Hydrogen exchange detection of discrete ligand-induced changes in hemoglobin.
    • ENGLANDER, S. W. & MAUEL, C. (1972). Hydrogen exchange detection of discrete ligand-induced changes in hemoglobin. J. Biol. Chem. 247, 2387–2394.
    • (1972) J. Biol. Chem. , vol.247 , pp. 2387-2394
    • ENGLANDER, S.W.1    MAUEL, C.2
  • 54
    • 84984086367 scopus 로고
    • Hydrogen-tritium exchange of the random chain polypeptide
    • ENGLANDER, S. W. & POULSEN, A. (1969). Hydrogen-tritium exchange of the random chain polypeptide. Biopolymers 7, 329–393.
    • (1969) Biopolymers , vol.7 , pp. 329-393
    • ENGLANDER, S.W.1    POULSEN, A.2
  • 55
    • 0015785662 scopus 로고
    • Structural and free energy changes in hemoglobin by use of a difference method
    • ENGLANDER, S. W. & ROLFE, A. (1973). Structural and free energy changes in hemoglobin by use of a difference method. J. Biol. Chem. 248, 4852–4861.
    • (1973) J. Biol. Chem. , vol.248 , pp. 4852-4861
    • ENGLANDER, S.W.1    ROLFE, A.2
  • 56
    • 0014694177 scopus 로고
    • Measurement of the free and the H-bonded amides of myoglobin
    • ENGLANDER, S. W. & STALEY, R. (1969). Measurement of the free and the H-bonded amides of myoglobin. J. molec. Biol. 45, 277—295.
    • (1969) J. molec. Biol. , vol.45 , pp. 277-295
    • ENGLANDER, S.W.1    STALEY, R.2
  • 57
    • 0019075326 scopus 로고
    • Solvent effects and polar interactions in the structural stability and dynamics of globular proteins.
    • FINNEY, J. L., GELLATLY, B. J., GOLTON, I. C. & GOODFELLOW, J. (1980). Solvent effects and polar interactions in the structural stability and dynamics of globular proteins. Biophys. J. 32, 17–30.
    • (1980) Biophys. J. , vol.32 , pp. 17-30
    • FINNEY, J.L.1    GELLATLY, B.J.2    GOLTON, I.C.3    GOODFELLOW, J.4
  • 58
    • 0019075327 scopus 로고
    • Structural dynamics of liganded myoglobin
    • FRAUENFELDER, H. & PETSKO, G. A. (1980). Structural dynamics of liganded myoglobin. Biophys. J. 32, 465–478.
    • (1980) Biophys. J. , vol.32 , pp. 465-478
    • FRAUENFELDER, H.1    PETSKO, G.A.2
  • 59
    • 0018793861 scopus 로고
    • Temperature dependent X-ray diffraction as a probe of protein structural dynamics
    • FRAUENFELDER, H., PETSKO, G. A. & TSERNOGLU, D. (1979). Temperature dependent X-ray diffraction as a probe of protein structural dynamics. Nature, Lond. 280, 558–563.
    • (1979) Nature, Lond. , vol.280 , pp. 558-563
    • FRAUENFELDER, H.1    PETSKO, G.A.2    TSERNOGLU, D.3
  • 60
    • 0017081495 scopus 로고
    • Rate of tritium labelling of specific purines in relation to nucleic acid and RNA conformation.
    • GAMBLE, R. C., SCHOEMAKER, H. J. P., JEKOWSKY, E. & SCHIMMEL, P. R. (1976). Rate of tritium labelling of specific purines in relation to nucleic acid and RNA conformation. Biochemistry 15, 2791–2799.
    • (1976) Biochemistry , vol.15 , pp. 2791-2799
    • GAMBLE, R.C.1    SCHOEMAKER, H.J.P.2    JEKOWSKY, E.3
  • 61
    • 0001144806 scopus 로고
    • Position dependent viscosity effects on rate coefficients
    • GAVISH, B. (1980). Position dependent viscosity effects on rate coefficients. Phys. Rev. Lett. 44, 1160–1163.
    • (1980) Phys. Rev. Lett. , vol.44 , pp. 1160-1163
    • GAVISH, B.1
  • 63
    • 0015518668 scopus 로고
    • On the conformation of tRNA in solution: dependence of denaturation temperature and structural parameters of mixed and formylmethionyl E. coli tRNA on sodium ion concentration.
    • GOLDSTEIN, R. N., STEFANOVIC, S. & KALLENBACH, N. R. (1972). On the conformation of tRNA in solution: dependence of denaturation temperature and structural parameters of mixed and formylmethionyl E. coli tRNA on sodium ion concentration. J. molec. Biol. 69, 217–236.
    • (1972) J. molec. Biol. , vol.69 , pp. 217-236
    • GOLDSTEIN, R.N.1    STEFANOVIC, S.2    KALLENBACH, N.R.3
  • 64
    • 0015914592 scopus 로고
    • Free energy of imperfect nucleic acid helices
    • GRALLA, J. & CROTHERS, D. M. (1973). Free energy of imperfect nucleic acid helices. J. molec. Biol. 73, 497–511.
    • (1973) J. molec. Biol. , vol.73 , pp. 497-511
    • GRALLA, J.1    CROTHERS, D.M.2
  • 65
    • 0020477028 scopus 로고
    • Thermodynamics of structural fluctuations in lysozyme as revealed by hydrogen exchange kinetics.
    • GREGORY, R. B., KNOX, D. G., PERCY, A. J. & ROSENBERG, A. (1982). Thermodynamics of structural fluctuations in lysozyme as revealed by hydrogen exchange kinetics. Biochemistry 21, 6523–6530.
    • (1982) Biochemistry , vol.21 , pp. 6523-6530
    • GREGORY, R.B.1    KNOX, D.G.2    PERCY, A.J.3    ROSENBERG, A.4
  • 67
    • 0001284259 scopus 로고
    • The ionization of water at high pressures
    • HAMANN, S. A. (1963). The ionization of water at high pressures. J. phys. Chem. 67, 2233–2235.
    • (1963) J. phys. Chem. , vol.67 , pp. 2233-2235
    • HAMANN, S.A.1
  • 68
    • 0020481577 scopus 로고
    • Direct assignment of the dihydrouridine-helix imino proton resonances in transfer ribonucleic acid nuclear magnetic resonance spectra by means of the nuclear overhauser effect.
    • HARE, D. R. & REID, B. R.(1982). Direct assignment of the dihydrouridine-helix imino proton resonances in transfer ribonucleic acid nuclear magnetic resonance spectra by means of the nuclear overhauser effect. Biochemistry 21, 1835–1842.
    • (1982) Biochemistry , vol.21 , pp. 1835-1842
    • HARE, D.R.1
  • 69
    • 0012154171 scopus 로고
    • Deuterium oxide solvent isotope effects on N-H… O, O-H… N and N-H… N intramolecular hydrogen bonds.
    • HASLAM, J. L. & EYRING, E. M. (1967). Deuterium oxide solvent isotope effects on N-H… O, O-H… N and N-H… N intramolecular hydrogen bonds. J. phys. Chem. 71, 4470–4475.
    • (1967) J. phys. Chem. , vol.71 , pp. 4470-4475
    • HASLAM, J.L.1    EYRING, E.M.2
  • 70
    • 0014671869 scopus 로고
    • Unfolding and hydrogen exchange of proteins: the three dimensional Ising lattice as a model.
    • HERMANS, J. JR., LOHR, D. & FERRO, D. (1969). Unfolding and hydrogen exchange of proteins: the three dimensional Ising lattice as a model. Nature, Lond. 224, 175–177.
    • (1969) Nature, Lond. , vol.224 , pp. 175-177
    • HERMANS, J.1    LOHR, D.2    FERRO, D.3
  • 71
    • 0017314027 scopus 로고
    • Dynamics of the basic pancreatic trypsin inhibitor (BPTI)
    • II. Semi-empirical energy calculations.
    • HETZEL, R., WUTHRICH, K., DEISENHOFER, J. & HUBER, R. (1976). Dynamics of the basic pancreatic trypsin inhibitor (BPTI). II. Semi-empirical energy calculations. Biophys. Struct. & Mechanism 2, 159–180.
    • (1976) Biophys. Struct. & Mechanism , vol.2 , pp. 159-180
    • HETZEL, R.1    WUTHRICH, K.2    DEISENHOFER, J.3    HUBER, R.4
  • 72
    • 0019872611 scopus 로고
    • Protein fluctuations limiting HX rates in the folded state are not correlated to thermal stability in denaturants
    • HILTON, D. B., TRUDEAU, K. R. & WOODWARD, C. K. (1981). Protein fluctuations limiting HX rates in the folded state are not correlated to thermal stability in denaturants. Biochemistry 20, 4697–4703.
    • (1981) Biochemistry , vol.20 , pp. 4697-4703
    • HILTON, D.B.1    TRUDEAU, K.R.2    WOODWARD, C.K.3
  • 73
    • 0017812083 scopus 로고
    • Nuclear magnetic resonance measurement of hydrogen exchange kinetics of single protons in basic pancreatic trypsin inhibitor
    • HILTON, B. D. & WOODWARD, C. K. (1978). Nuclear magnetic resonance measurement of hydrogen exchange kinetics of single protons in basic pancreatic trypsin inhibitor. Biochemistry 17, 3325–3332.
    • (1978) Biochemistry , vol.17 , pp. 3325-3332
    • HILTON, B.D.1    WOODWARD, C.K.2
  • 74
    • 0018801594 scopus 로고
    • On the mechanism of isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor.
    • HILTON, B. D. & WOODWARD, C. K. (1979). On the mechanism of isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor. Biochemistry 18, 5834–5841.
    • (1979) Biochemistry , vol.18 , pp. 5834-5841
    • HILTON, B.D.1    WOODWARD, C.K.2
  • 76
    • 0020647920 scopus 로고
    • Functional significance of flexibility in proteins.
    • HUBER, R. & BENNETT, W. S. JR. (1983). Functional significance of flexibility in proteins. Biopolymers 22, 261–279.
    • (1983) Biopolymers , vol.22 , pp. 261-279
    • HUBER, R.1    BENNETT, W.S.2
  • 78
    • 0019171506 scopus 로고
    • Helix-coil dynamics in RNA: the amino acid acceptor helix of phenylalanine transfer RNA
    • HURD, R. E. & REID, B. R. (1980). Helix-coil dynamics in RNA: the amino acid acceptor helix of phenylalanine transfer RNA. J. molec. Biol. 142, 181–194.
    • (1980) J. molec. Biol. , vol.142 , pp. 181-194
    • HURD, R.E.1    REID, B.R.2
  • 79
    • 0001042982 scopus 로고
    • Discussion of the pH dependence of the H-D exchange of proteins
    • HVIDT, A. (1964). Discussion of the pH dependence of the H-D exchange of proteins. C. r. Trav. Lab. Carlsberg 34, 299–317.
    • (1964) C. r. Trav. Lab. Carlsberg , vol.34 , pp. 299-317
    • HVIDT, A.1
  • 80
    • 84889616385 scopus 로고
    • Isotopic hydrogen exchange in solutions of biological macromolecules
    • (ed. C. Sadron, Holland: Reidel.
    • HVIDT, A. (1973). Isotopic hydrogen exchange in solutions of biological macromolecules. In Dynamic Aspects of Conformational Changes in Macromolecules (ed. C. Sadron), pp. 103–115. Holland: Reidel.
    • (1973) Dynamic Aspects of Conformational Changes in Macromolecules , pp. 103-115
    • HVIDT, A.1
  • 81
    • 33947296801 scopus 로고
    • Kinetics of hydrogen-deuterium exchange in poly-Af-vinylacetamide measured by infrared spectroscopy.
    • HVIDT, A. & CORETT, R. (1970). Kinetics of hydrogen-deuterium exchange in poly-Af-vinylacetamide measured by infrared spectroscopy. J. Am. chem. Soc. 92, 5546-5556.
    • (1970) J. Am. chem. Soc. , vol.92 , pp. 5556
    • HVIDT, A.1    CORETT, R.2
  • 82
    • 0000277207 scopus 로고
    • Exchange of hydrogen atoms in insulin with deuterium atoms in aqueous solutions
    • HVIDT, A. & LINDERSTRDM-LANG, K. (1954). Exchange of hydrogen atoms in insulin with deuterium atoms in aqueous solutions. Biochim. biophys. Acta 14, 574-575.
    • (1954) Biochim. biophys. Acta , vol.14 , pp. 574-575
    • HVIDT, A.1    LINDERSTRDM-LANG, K.2
  • 83
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • HVIDT, A. & NIELSEN, S. O. (1966). Hydrogen exchange in proteins. Adv. Protein Chem. 21, 287–386.
    • (1966) Adv. Protein Chem. , vol.21 , pp. 287-386
    • HVIDT, A.1    NIELSEN, S.O.2
  • 84
    • 0015500463 scopus 로고
    • Conformational changes in human serum albumin as revealed by hydrogen deuterium exchange studies
    • HVIDT, A. & WALLEVIK, K. (1972). Conformational changes in human serum albumin as revealed by hydrogen deuterium exchange studies. J. biol. Chem. 247, 1530-535.
    • (1972) J. biol. Chem. , vol.247 , pp. 1530-1535
    • HVIDT, A.1    WALLEVIK, K.2
  • 85
    • 84966157142 scopus 로고
    • Isotope exchange and conformational fluctuation in polypeptides
    • IKEGAMI, A., KANEHISA, M. I., NAKANISHI, M. & TSUBOI, M. (1974). Isotope exchange and conformational fluctuation in polypeptides. Adv. Biophys 6, 1–39.
    • (1974) Adv. Biophys , vol.6 , pp. 1-39
    • IKEGAMI, A.1    KANEHISA, M.I.2    NAKANISHI, M.3    TSUBOI, M.4
  • 86
    • 33750443227 scopus 로고
    • Tritium-hydrogen exchange of polypeptides in aqueous solutions.
    • IKEGAMI, A. & KONO, N. (1967). Tritium-hydrogen exchange of polypeptides in aqueous solutions. J. molec. Biol. 29, 251–274.
    • (1967) J. molec. Biol. , vol.29 , pp. 251-274
    • IKEGAMI, A.1    KONO, N.2
  • 87
    • 0019874692 scopus 로고
    • Study of ribonucleic acid unfolding by dynamic nuclear magnetic resonance
    • JOHNSTON, P. D. & REDFIELD, A. G. (1981). Study of ribonucleic acid unfolding by dynamic nuclear magnetic resonance. Biochemistry 20, 3996–4006.
    • (1981) Biochemistry , vol.20 , pp. 3996-4006
    • JOHNSTON, P.D.1    REDFIELD, A.G.2
  • 88
    • 0019872824 scopus 로고
    • The role of proline residues in the folding kinetics of the bovine pancreatic trypsin inhibitor derivative RCAM (14–38)
    • JULLIEN, M. & BALDWIN, R. L. (1981). The role of proline residues in the folding kinetics of the bovine pancreatic trypsin inhibitor derivative RCAM (14–38). J. Molec. Biol. 145, 265–280.
    • (1981) J. Molec. Biol. , vol.145 , pp. 265-280
    • JULLIEN, M.1    BALDWIN, R.L.2
  • 89
    • 13344292340 scopus 로고
    • Hydrogen-deuterium exchange of a charged poly-methacrylamide and its monomeric analog.
    • KAKUDA, Y., PERRY, N. & MUELLER, D. D. (1971). Hydrogen-deuterium exchange of a charged poly-methacrylamide and its monomeric analog. J. Am. chem. Soc. 93, 5992–5998.
    • (1971) J. Am. chem. Soc. , vol.93 , pp. 5992-5998
    • KAKUDA, Y.1    PERRY, N.2    MUELLER, D.D.3
  • 90
    • 84976137000 scopus 로고
    • Effects of bases on fluctuations at the heme pocket of cyanometmyoglobin
    • (in the Press).
    • KALLENBACH, N. R. & KIM, P. S. (1984). Effects of bases on fluctuations at the heme pocket of cyanometmyoglobin. Proc. natn. Acad. Sci. U.S.A. (in the Press).
    • (1984) Proc. natn. Acad. Sci. U.S.A.
    • KALLENBACH, N.R.1    KIM, P.S.2
  • 92
  • 93
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • KAUZMANN, W. (1959). Some factors in the interpretation of protein denaturation. Adv. Protein Chem. 14, 1–63.
    • (1959) Adv. Protein Chem. , vol.14 , pp. 1-63
    • KAUZMANN, W.1
  • 94
    • 0013411169 scopus 로고
    • Molecular mechanical studies of DNA flexibility: Coupled backbone torsion angles and base-pair openings
    • KEEPERS, J. W., KOLLMAN, P. A., WEINER, P. K. & JAMES, T. L. (1982). Molecular mechanical studies of DNA flexibility: Coupled backbone torsion angles and base-pair openings. Proc. natn. Acad. Sci. U.S.A. 79, 5537-5541.
    • (1982) Proc. natn. Acad. Sci. U.S.A. , vol.79 , pp. 5537-5541
    • KEEPERS, J.W.1    KOLLMAN, P.A.2    WEINER, P.K.3    JAMES, T.L.4
  • 95
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reaction of small proteins and the mechanism of protein folding.
    • KIM, P. S. & BALDWIN, R. L. (1982). Specific intermediates in the folding reaction of small proteins and the mechanism of protein folding. A. Rev. Biochem. 51, 459–489.
    • (1982) A. Rev. Biochem. , vol.51 , pp. 459-489
    • KIM, P.S.1    BALDWIN, R.L.2
  • 96
    • 0020475145 scopus 로고
    • Influence of charge on the rate of amide proton exchange
    • KIM, P. S. & BALDWIN, R. L. (1982). Influence of charge on the rate of amide proton exchange. Biochemistry 21, 1–5.
    • (1982) Biochemistry , vol.21 , pp. 1-5
    • KIM, P.S.1    BALDWIN, R.L.2
  • 97
    • 70449538832 scopus 로고
    • Non-covalent bonds in protein structure
    • KLOTZ, I. M. (1960). Non-covalent bonds in protein structure. Brookhaven Symp. Biol. 13, 25–48.
    • (1960) Brookhaven Symp. Biol. , vol.13 , pp. 25-48
    • KLOTZ, I.M.1
  • 98
    • 0019011405 scopus 로고
    • Fluctuations of protein structure as expressed in the distribution of hydrogen exchange rate constants
    • KNOX, D. & ROSENBERG, A. (1980). Fluctuations of protein structure as expressed in the distribution of hydrogen exchange rate constants. Biopolymers 19, 1049–1068.
    • (1980) Biopolymers , vol.19 , pp. 1049-1068
    • KNOX, D.1    ROSENBERG, A.2
  • 99
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • KOSHLAND, D. E., jr., NEMETHY, G. & filmer, D. (1966). Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5, 365–385.
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • KOSHLAND, D.E.1    NEMETHY, G.2    filmer, D.3
  • 100
    • 0020488766 scopus 로고
    • Protein dynamics investigated by the neutron diffraction-hydrogen exchange technique
    • KOSSIAKOFF, A. A. (1982). Protein dynamics investigated by the neutron diffraction-hydrogen exchange technique. Nature, Lond. 296, 713–721.
    • (1982) Nature, Lond. , vol.296 , pp. 713-721
    • KOSSIAKOFF, A.A.1
  • 101
    • 0019491881 scopus 로고
    • Anomalous exchange kinetics of peptide amide protons in aqueous solution.
    • KRAUSS, E. M. & COWBURN, D. (1981). Anomalous exchange kinetics of peptide amide protons in aqueous solution. Int. J. Peptide & Protein Res. 17, 42-47.
    • (1981) Int. J. Peptide & Protein Res. , vol.17 , pp. 42-47
    • KRAUSS, E.M.1    COWBURN, D.2
  • 102
    • 0021095604 scopus 로고
    • Exchange behavior of the H-bonded amide protons in the 3 – 13 helix of ribonuclease S.
    • KUWAJIMA, K. & BALDWIN, R. L. (1983). Exchange behavior of the H-bonded amide protons in the 3 – 13 helix of ribonuclease S. J. molec. Biol. 169, 299–324.
    • (1983) J. molec. Biol. , vol.169 , pp. 299-324
    • KUWAJIMA, K.1    BALDWIN, R.L.2
  • 103
    • 0015907980 scopus 로고
    • Quenching of fluorescence by oxygen.
    • A probe for structural fluctuations in macromolecules
    • LAKOWICZ, J. R. & WEBER, G. (1973). Quenching of fluorescence by oxygen. A probe for structural fluctuations in macromolecules. Biochemistry 12, 4161–4170.
    • (1973) Biochemistry , vol.12 , pp. 4161-4170
    • LAKOWICZ, J.R.1    WEBER, G.2
  • 104
    • 0015895751 scopus 로고
    • Quenching of protein fluorescence by oxygen
    • Detection of structural fluctuations in proteins on the nanosecond time scale
    • LAKOWICZ, J. R. & WEBER, G. (1973). Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry 12, 4171–4179.
    • (1973) Biochemistry , vol.12 , pp. 4171-4179
    • LAKOWICZ, J.R.1    WEBER, G.2
  • 105
    • 0018781485 scopus 로고
    • Kinetics of hydrogen-deuterium exchange in GMP and cyclic GMP determined by laser Raman spectroscopy.
    • LANE, M. J. & THOMAS, G. J. JR (1979). Kinetics of hydrogen-deuterium exchange in GMP and cyclic GMP determined by laser Raman spectroscopy. Biochemistry 18, 3839–3846.
    • (1979) Biochemistry , vol.18 , pp. 3839-3846
    • LANE, M.J.1    THOMAS, G.J.2
  • 106
    • 0015222647 scopus 로고
    • The interpretation of protein structures: estimation of static accessibility.
    • LEE, B. & RICHARDS, F. M. (1971). The interpretation of protein structures: estimation of static accessibility. J. molec. Biol. 55, 379–440.
    • (1971) J. molec. Biol. , vol.55 , pp. 379-440
    • LEE, B.1    RICHARDS, F.M.2
  • 107
    • 13044299926 scopus 로고
    • Catalysis of H—D exchange in polypeptides
    • LEICHTLING, B. H. & KLOTZ, I. M. (1966). Catalysis of H—D exchange in polypeptides. Biochemistry 5, 4026–4036.
    • (1966) Biochemistry , vol.5 , pp. 4026-4036
    • LEICHTLING, B.H.1    KLOTZ, I.M.2
  • 108
    • 0000014361 scopus 로고
    • Origin of the absorption band at 1550 cm-1in proteins.
    • LENORMANT, H. & BLOUT, E. R. (1953). Origin of the absorption band at 1550 cm-1in proteins. Nature, Lortd. 172, 720–722.
    • (1953) Nature, Lortd. , vol.172 , pp. 720-722
    • LENORMANT, H.1    BLOUT, E.R.2
  • 109
    • 0019774669 scopus 로고
    • Molecular dynamics of hydrogen bonds in bovine pancreatic trypsin inhibitor protein
    • LEVITT, M. (1981a). Molecular dynamics of hydrogen bonds in bovine pancreatic trypsin inhibitor protein. Nature, Lond. 294, 379–380.
    • (1981) Nature, Lond. , vol.294 , pp. 379-380
    • LEVITT, M.1
  • 110
    • 84985468629 scopus 로고
    • Hydrogen bond and internal solvent dynamics of BPTI protein
    • LEVITT, M. (1981). Hydrogen bond and internal solvent dynamics of BPTI protein. Ann. N.Y. Acad. Sci. 367, 162–181.
    • (1981) Ann. N.Y. Acad. Sci. , vol.367 , pp. 162-181
    • LEVITT, M.1
  • 111
    • 0020011210 scopus 로고
    • Protein conformation, dynamics and folding by computer simulation.
    • LEVITT, M. (1982). Protein conformation, dynamics and folding by computer simulation. A. Rev. Biophys. Bioeng. 11, 251–271.
    • (1982) A. Rev. Biophys. Bioeng. , vol.11 , pp. 251-271
    • LEVITT, M.1
  • 112
    • 84975947808 scopus 로고
    • Molecular dynamics of native protein.
    • in the Press
    • LEVITT, M. (1983). Molecular dynamics of native protein. J. molec. Biol. (in the Press).
    • (1983) J. molec. Biol.
    • LEVITT, M.1
  • 113
    • 0017309766 scopus 로고
    • Structural patterns in globular proteins.
    • LEVITT, M. & CHOTHIA, C. (1976). Structural patterns in globular proteins. Nature, Lond. 261, 552–557.
    • (1976) Nature, Lond. , vol.261 , pp. 552-557
    • LEVITT, M.1    CHOTHIA, C.2
  • 114
    • 0019877458 scopus 로고
    • Carbon-13 spin lattice relaxation, linewidth and nuclear overhauser enhancement measurements of nucleosome length DNA.
    • LEVY, G., HILLIARD, P. R., LEVY, L. F. & RILL, R. L. (1981). Carbon-13 spin lattice relaxation, linewidth and nuclear overhauser enhancement measurements of nucleosome length DNA. J. Biol. Chem. 256, 9986–9989.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9986-9989
    • LEVY, G.1    HILLIARD, P.R.2    LEVY, L.F.3    RILL, R.L.4
  • 115
    • 84985649741 scopus 로고
    • Vibrational approaches to the dynamics of an alpha-helix
    • LEVY, R. M. & KARPLUS, M. (1979). Vibrational approaches to the dynamics of an alpha-helix.Biopolymers 18, 2465–2495.
    • (1979) Biopolymers , vol.18 , pp. 2465-2495
    • LEVY, R.M.1    KARPLUS, M.2
  • 116
    • 0001917325 scopus 로고
    • Deuterium exchange between peptides and water
    • InSymposium on Peptide Chemistry
    • LINDERSTRGM-LANG, K. U. (1955). Deuterium exchange between peptides and water. InSymposium on Peptide Chemistry. Chem. Soc. Spec. Puhl. 2, 1–20.
    • (1955) Chem. Soc. Spec. Puhl. , vol.2 , pp. 1-20
    • LINDERSTRGM-LANG, K.U.1
  • 117
    • 0037644405 scopus 로고
    • Deuterium exchange and protein structure
    • (ed. A. Neuberger). London: Methuen
    • LINDERSTROM-LANG, K. U. (1958). Deuterium exchange and protein structure. In Symposium on Protein Structure (ed. A. Neuberger). London: Methuen.
    • (1958) Symposium on Protein Structure
    • LINDERSTROM-LANG, K.U.1
  • 118
    • 0000013948 scopus 로고
    • Protein structure and enzyme activity
    • 2nd ed., (ed. P. D. Boyer, H. Lardy and K. Myrback). New York: Academic Press
    • LINDERSTROM-LANG, K. U. & SCHELLMAN, J. A. (1959). Protein structure and enzyme activity. In The Enzymes, 2nd ed. vol. 1 (ed. P. D. Boyer, H. Lardy and K. Myrback). New York: Academic Press.
    • (1959) The Enzymes , vol.1
    • LINDERSTROM-LANG, K.U.1    SCHELLMAN, J.A.2
  • 119
    • 0015919121 scopus 로고
    • The solution conformation of the ferrichromes
    • LLINAS, M., KLEIN, M. P. & NEILANDS, J. B. (1973a). The solution conformation of the ferrichromes. J. Biol. Chem. 248, 915–923.
    • (1973) J. Biol. Chem. , vol.248 , pp. 915-923
    • LLINAS, M.1    KLEIN, M.P.2    NEILANDS, J.B.3
  • 120
    • 0015919148 scopus 로고
    • The solution conformation of the ferrichromes
    • LLINAS, M., KLEIN, M. P. & NEILANDS, J. B. (1973). The solution conformation of the ferrichromes. J. Biol. Chem. 248, 924–931.
    • (1973) J. Biol. Chem. , vol.248 , pp. 924-931
    • LLINAS, M.1    KLEIN, M.P.2    NEILANDS, J.B.3
  • 121
    • 0016416847 scopus 로고
    • Structural and energetic consequences of non-complementary base oppositions in nucleic acids
    • LOMANT, A. J. & FRESCO, J. R. (1975). Structural and energetic consequences of non-complementary base oppositions in nucleic acids. Prog. nucleic Acid Res. & molec. Biol. 15, 185—218.
    • (1975) Prog. nucleic Acid Res. & molec. Biol. , vol.15 , pp. 185-218
    • LOMANT, A.J.1    FRESCO, J.R.2
  • 122
    • 84976106497 scopus 로고
    • The role of conformational fluctuations in protein association, immunology and tissue recognition.
    • (ed. N. Imai and S. Sugai). Kyoto. (In the Press.)
    • LUMRY, R. (1978). The role of conformational fluctuations in protein association, immunology and tissue recognition. In Dynamic Properties of Polyion Systems (ed. N. Imai and S. Sugai). Kyoto. (In the Press.)
    • (1978) Dynamic Properties of Polyion Systems
    • LUMRY, R.1
  • 123
    • 84984083911 scopus 로고
    • The dynamics of the helix-coil transition in poly-glutamic acid
    • LUMRY, R., LEGARE, R. & MILLER, W. G. (1964). The dynamics of the helix-coil transition in poly-glutamic acid. Biopolymers 2, 489–500.
    • (1964) Biopolymers , vol.2 , pp. 489-500
    • LUMRY, R.1    LEGARE, R.2    MILLER, W.G.3
  • 126
    • 0018796418 scopus 로고
    • Picosecond dynamics of tyrosine side chains in proteins
    • MCCAMMON, J. A., WOLYNES, P. G. & KARPLUS, M. (1979). Picosecond dynamics of tyrosine side chains in proteins. Biochemistry 18, 927–942.
    • (1979) Biochemistry , vol.18 , pp. 927-942
    • MCCAMMON, J.A.1    WOLYNES, P.G.2    KARPLUS, M.3
  • 127
    • 0014945046 scopus 로고
    • Hydrogen exchange as a probe of the dynamic structure of DNA
    • MCCONNELL, B. M. & VON HIPPEL, P. H. (1970). Hydrogen exchange as a probe of the dynamic structure of DNA. J. molec. Biol. 50, 317–332.
    • (1970) J. molec. Biol. , vol.50 , pp. 317-332
    • MCCONNELL, B.M.1    VON HIPPEL, P.H.2
  • 128
    • 0016175688 scopus 로고
    • A general exchange mechanism.
    • Imidazole catalysis of amino proton exchange in 2,3 cyclic AMP.
    • MCCONNELL, B. (1974). Imidazole catalysis of amino proton exchange in 2,3 cyclic AMP. A general exchange mechanism. Biochemistry 13, 4516-4523
    • (1974) Biochemistry , vol.13 , pp. 4516-4523
    • MCCONNELL, B.1
  • 129
    • 0016694032 scopus 로고
    • Formaldehyde as a probe of DNA structure.
    • MCGHEE, J. D. & VON HIPPEL, P. H. (1975). Formaldehyde as a probe of DNA structure. Biochemistry 14, 1281–1303.
    • (1975) Biochemistry , vol.14 , pp. 1281-1303
    • MCGHEE, J.D.1    VON HIPPEL, P.H.2
  • 130
    • 0018146009 scopus 로고
    • Is protein turnover thermodynamically controlled?
    • MCLENDON, G. & RADANY, E. (1978). Is protein turnover thermodynamically controlled? J. biol. Chem. 253, 6335–6337.
    • (1978) J. biol. Chem. , vol.253 , pp. 6335-6337
    • MCLENDON, G.1    RADANY, E.2
  • 131
    • 0019185339 scopus 로고
    • The slowest allosterically responsive hydrogens in hemoglobin: completion of the hydrogen exchange survey
    • MALIN, E. L. & ENGLANDER, S. W. (1980). The slowest allosterically responsive hydrogens in hemoglobin: completion of the hydrogen exchange survey. J. biol. Chem. 255, 10695–10701.
    • (1980) J. biol. Chem. , vol.255 , pp. 10695-10701
    • MALIN, E.L.1    ENGLANDER, S.W.2
  • 132
    • 0018622828 scopus 로고
    • Base-pair opening and closing reactions in the double helix
    • MANDAL, C., KALLENBACH, N. R. & ENGLANDER, S. W. (1979). Base-pair opening and closing reactions in the double helix. J. molec. Biol. 135, 391–411.
    • (1979) J. molec. Biol. , vol.135 , pp. 391-411
    • MANDAL, C.1    KALLENBACH, N.R.2    ENGLANDER, S.W.3
  • 133
    • 0017091519 scopus 로고
    • Nuclear magnetic resonance determination of intramolecular distances in bovine pancreatic trypsin inhibitor using nitrotyrosine chelation of lanthanides
    • MARINETTI, T. D., SNYDER, G. H. & SYKES, B. D. (1976). Nuclear magnetic resonance determination of intramolecular distances in bovine pancreatic trypsin inhibitor using nitrotyrosine chelation of lanthanides. Biochemistry 15, 4600–4608.
    • (1976) Biochemistry , vol.15 , pp. 4600-4608
    • MARINETTI, T.D.1    SNYDER, G.H.2    SYKES, B.D.3
  • 135
    • 0021099323 scopus 로고
    • The pH dependence of hydrogen exchange in proteins.
    • in the Press
    • MATTHEW, J. B. & RICHARDS, F. M. (1983). The pH dependence of hydrogen exchange in proteins. J. biol. Chem. (in the Press).
    • (1983) J. biol. Chem.
    • MATTHEW, J.B.1    RICHARDS, F.M.2
  • 136
    • 0000525413 scopus 로고
    • Torsion and bending of nucleic acids studied by subnanosecond time resolved fluorescence depolarization of intercalated dyes
    • MILLAR, D. P., ROBBINS, R. J. & ZEWAIL, A. H. (1982). Torsion and bending of nucleic acids studied by subnanosecond time resolved fluorescence depolarization of intercalated dyes. J. chem. Phys. 76, 2080–2086.
    • (1982) J. chem. Phys. , vol.76 , pp. 2080-2086
    • MILLAR, D.P.1    ROBBINS, R.J.2    ZEWAIL, A.H.3
  • 137
    • 4344575233 scopus 로고
    • Hydrogen-deuterium exchange in some polymer amides
    • MILLER, M. M. & KLOTZ, I. M. (1973). Hydrogen-deuterium exchange in some polymer amides. J. Am. chem. Soc. 95, 5694–5700.
    • (1973) J. Am. chem. Soc. , vol.95 , pp. 5694-5700
    • MILLER, M.M.1    KLOTZ, I.M.2
  • 138
    • 84976107803 scopus 로고
    • 2nd ed., Oxford: Pergamon
    • MOELWYN-HUGHES, E. A. (1961). Physical Chemistry, 2nd ed., chapter 11, pp. 27–91. Oxford: Pergamon.
    • (1961) Physical Chemistry , vol.11 , pp. 27-91
    • MOELWYN-HUGHES, E.A.1
  • 139
    • 0015514380 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • MOLDAY, R. S., ENGLANDER, S. W. & KALLEN, R. G. (1972). Primary structure effects on peptide group hydrogen exchange. Biochemistry 11, 150–158.
    • (1972) Biochemistry , vol.11 , pp. 150-158
    • MOLDAY, R.S.1    ENGLANDER, S.W.2    KALLEN, R.G.3
  • 140
    • 84975951950 scopus 로고
    • On the nature of allosteric transitions: a plausible model.
    • MONOD, J., WYMAN, J. & CHANGEUX, J. P. (1965). On the nature of allosteric transitions: a plausible model. J. molec. Biol. 12, 33–118.
    • (1965) J. molec. Biol. , vol.12 , pp. 33-118
    • MONOD, J.1    WYMAN, J.2    CHANGEUX, J.P.3
  • 141
    • 0039539351 scopus 로고
    • Measurement of hydrogen exchange at the tryptophan residues of a protein by stopped flow and U V spectroscopy.
    • NAKANISHI, M., NAKAMURA, H., HIRAKAWA, A. Y., TSUBOI, M., NAGAMURA, T. & SAIJO, Y. (1978). Measurement of hydrogen exchange at the tryptophan residues of a protein by stopped flow and U V spectroscopy. J. Am. chem. Soc. 100, 272–276.
    • (1978) J. Am. chem. Soc. , vol.100 , pp. 272-276
    • NAKANISHI, M.1    NAKAMURA, H.2    HIRAKAWA, A.Y.3    TSUBOI, M.4    NAGAMURA, T.5    SAIJO, Y.6
  • 142
    • 0015527454 scopus 로고
    • Fluctuation of the lysozyme structure.
    • NAKANISHI, M., TSUBOI, M. & IKEGAMI, A. (1972). Fluctuation of the lysozyme structure. J. molec. Biol. 70, 351–361.
    • (1972) J. molec. Biol. , vol.70 , pp. 351-361
    • NAKANISHI, M.1    TSUBOI, M.2    IKEGAMI, A.3
  • 143
    • 0015935491 scopus 로고
    • Fluctuations of the lysozome structure.
    • Effects of temperature and binding of inhibitors.
    • NAKANISHI, M., TSUBOI, M. & IKEGAMI, A. (1973). Fluctuations of the lysozome structure. II. Effects of temperature and binding of inhibitors. J. Molec. BioL 75, 673–682.
    • (1973) J. Molec. BioL , vol.75 , Issue.2 , pp. 673-682
    • NAKANISHI, M.1    TSUBOI, M.2    IKEGAMI, A.3
  • 145
    • 0015505535 scopus 로고
    • Fluctuation of an alpha-helix structure. Difference between the central and terminal portions.
    • NAKANISHI, M., TSUBOI, M., IKEGAMI, A. & KANESHISA, M. (1972). Fluctuation of an alpha-helix structure. Difference between the central and terminal portions. J. molec. Biol. 64, 363–378.
    • (1972) J. molec. Biol. , vol.64 , pp. 363-378
    • NAKANISHI, M.1    TSUBOI, M.2    IKEGAMI, A.3    KANESHISA, M.4
  • 146
    • 0020488742 scopus 로고
    • Collective variable description of small amplitude conformational fluctuations in a globular protein.
    • NOGUTI, T. & GO, N. (1982). Collective variable description of small amplitude conformational fluctuations in a globular protein. Nature, Lond. 296, 776–778.
    • (1982) Nature, Lond. , vol.296 , pp. 776-778
    • NOGUTI, T.1    GO, N.2
  • 147
    • 0016505899 scopus 로고
    • The stability of globular proteins
    • PACE, C. W. (1975). The stability of globular proteins. C.R.C. Crit. Revs. Biochem. 3, 1–43.
    • (1975) C.R.C. Crit. Revs. Biochem. , vol.3 , pp. 1-43
    • PACE, C.W.1
  • 148
    • 0020477029 scopus 로고
    • Kinetics of exchange of imino protons in the d(C-G-C-G-A-A-T-T-C-G-C-G) double helix and in two similar helices that contain a G. T base pair d(C-G-T-G-A-A-T-T-C-G-C-G), and an extra adenine d(C-G-C-A-G-A-A-T-T-C-G-C-G).
    • PARDI, A., MORDEN, K. M., PATEL, D. J. & TINOCO, I., JR. (1982). Kinetics of exchange of imino protons in the d(C-G-C-G-A-A-T-T-C-G-C-G) double helix and in two similar helices that contain a G. T base pair d(C-G-T-G-A-A-T-T-C-G-C-G), and an extra adenine d(C-G-C-A-G-A-A-T-T-C-G-C-G). Biochemistry 24, 6567–6574.
    • (1982) Biochemistry , vol.24 , pp. 6567-6574
    • PARDI, A.1    MORDEN, K.M.2    PATEL, D.J.3    TINOCO, I.4
  • 149
    • 0020482334 scopus 로고
    • Kinetics for exchange of imino protons in DNA, RNA, and hybrid oligonucleotide helices
    • PARDI, A. & TINOCO, I., jr. (1982). Kinetics for exchange of imino protons in DNA, RNA, and hybrid oligonucleotide helices. Biochemistry 21, 4686–4693.
    • (1982) Biochemistry , vol.21 , pp. 4686-4693
    • PARDI, A.1    TINOCO, I.2
  • 150
    • 0020476728 scopus 로고
    • DNA conformation, dynamics, and interactions in solution.
    • PATEL, D. J., PARDI, A. & ITAKURA, K. (1982). DNA conformation, dynamics, and interactions in solution. Science, N.Y. 216, 581–590.
    • (1982) Science, N.Y. , vol.216 , pp. 581-590
    • PATEL, D.J.1    PARDI, A.2    ITAKURA, K.3
  • 151
    • 0000942596 scopus 로고
    • Stereochemistry of cooperative effects in hemoglobin.
    • PERUTZ, M. F.(1980). Stereochemistry of cooperative effects in hemoglobin. Nature, Lond. 228, 726–739.
    • (1980) Nature, Lond. , vol.228 , pp. 726-739
    • PERUTZ, M.F.1
  • 153
    • 0019752345 scopus 로고
    • Crystallographic studies of movement within proteins
    • PHILLIPS, D. C. (1981). Crystallographic studies of movement within proteins. Biochem. Soc. Symp. 46, 1–15.
    • (1981) Biochem. Soc. Symp. , vol.46 , pp. 1-15
    • PHILLIPS, D.C.1
  • 154
    • 0020648391 scopus 로고
    • Sequential hydration of a dry globular protein
    • POOLE, P. L. & FINNEY, J. L. (1983). Sequential hydration of a dry globular protein. Biopolymers 22, 255–260.
    • (1983) Biopolymers , vol.22 , pp. 255-260
    • POOLE, P.L.1    FINNEY, J.L.2
  • 155
    • 0014301563 scopus 로고
    • Comparison of protein structure in the crystal and in solution
    • II. Tritium hydrogen exchange of zinc-free and zinc insulin.
    • PRAISSMAN, M. & RUPLEY, J. A. (1968a). Comparison of protein structure in the crystal and in solution. II. Tritium hydrogen exchange of zinc-free and zinc insulin. Biochemistry 7, 2431–2445.
    • (1968) Biochemistry , vol.7 , pp. 2431-2445
    • PRAISSMAN, M.1    RUPLEY, J.A.2
  • 157
    • 84976106492 scopus 로고
    • Equilibrium and kinetic characteristics of the low temperature open state in polynucleotide duplexes.
    • New York: Adenine Press
    • PREISLER, R. S., MANDAL, C., ENGLANDER, S. W., KALLENBACH, N. R., HOWARD, F. B., FRAZIER, J. & MILES, H. T. (1981). Equilibrium and kinetic characteristics of the low temperature open state in polynucleotide duplexes. In Biomolecular Stereodynamics (ed. R. H. Sarma), pp. 405–415. New York: Adenine Press.
    • (1981) Biomolecular Stereodynamics , pp. 405-415
    • PREISLER, R.S.1    MANDAL, C.2    ENGLANDER, S.W.3    KALLENBACH, N.R.4    HOWARD, F.B.5    FRAZIER, J.6    MILES, H.T.7
  • 159
    • 0018588511 scopus 로고
    • Stability of proteins
    • PRIVALOV, P. L. (1979). Stability of proteins. Adv. Protein Chem. 33, 167–241.
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • PRIVALOV, P.L.1
  • 160
    • 0019348708 scopus 로고
    • NMR studies on RNA structure and dynamics
    • REID, B. R. (1981). NMR studies on RNA structure and dynamics. A. Rev. Biochem. 50, 969–996.
    • (1981) A. Rev. Biochem. , vol.50 , pp. 969-996
    • REID, B.R.1
  • 161
    • 0007064136 scopus 로고
    • Thermodynamics and Thermochemistry of Biologically Important Systems
    • MTP Butterworths
    • RIALDI, G. & BILTONEN, R. L. (1975). Thermodynamics and Thermochemistry of Biologically Important Systems, MTP 1st Rev. Sci., pp. 148–184. MTP Butterworths.
    • (1975) MTP 1st Rev. Sci. , pp. 148-184
    • RIALDI, G.1    BILTONEN, R.L.2
  • 162
    • 0002278852 scopus 로고
    • Packing defects, cavities, volume fluctuations, and access to the interior of proteins.
    • RICHARDS, F. M. (1979). Packing defects, cavities, volume fluctuations, and access to the interior of proteins. Carlsherg Res. Commun. 44, 47–63.
    • (1979) Carlsherg Res. Commun. , vol.44 , pp. 47-63
    • RICHARDS, F.M.1
  • 163
    • 84965093921 scopus 로고
    • The preparation of subtilisin-modified ribonuclease and the separation of the peptide and protein components
    • RICHARDS, F. M. & VITHAYATHIL, P. J. (1959). The preparation of subtilisin-modified ribonuclease and the separation of the peptide and protein components. J. biol. Chem. 234,.1459–1465
    • (1959) J. biol. Chem. , vol.234 , pp. 1459-1465
    • RICHARDS, F.M.1    VITHAYATHIL, P.J.2
  • 164
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • RICHARDSON, J. (1979). The anatomy and taxonomy of protein structure. Adv. Protein Chem. 34, 167–339.
    • (1979) Adv. Protein Chem. , vol.34 , pp. 167-339
    • RICHARDSON, J.1
  • 165
    • 0018782055 scopus 로고
    • Kinetics of the exchange of individual amide protons in the basic pancreatic trypsin inhibitor.
    • RICHARZ, R., SEHR, P., WAGNER, G. & WUTHRICH, K. (1979). Kinetics of the exchange of individual amide protons in the basic pancreatic trypsin inhibitor. J. molec. Biol. 130, 19—30
    • (1979) J. molec. Biol. , vol.130 , pp. 19-30
    • RICHARZ, R.1    SEHR, P.2    WAGNER, G.3    WUTHRICH, K.4
  • 166
    • 0018794764 scopus 로고
    • Structural characterization by nuclear magnetic resonance of a reactive site carbon-13 labelled basic pancreatic trypsin inhibitor with the peptide bond Arg-39-Ala-40 cleaved and Arg-39 removed.
    • RICHARZ, R., TSCHESCHE, H. & WUTHRICH, J. (1979). Structural characterization by nuclear magnetic resonance of a reactive site carbon-13 labelled basic pancreatic trypsin inhibitor with the peptide bond Arg-39-Ala-40 cleaved and Arg-39 removed. Eur. J. Biochem. 102, 563–571.
    • (1979) Eur. J. Biochem. , vol.102 , pp. 563-571
    • RICHARZ, R.1    TSCHESCHE, H.2    WUTHRICH, J.3
  • 167
    • 84976059251 scopus 로고
    • Mobilitat in Proteinen unter nativen und denaturierden Bedingungen: Untersuchung von Trypsin Inhibitoren mit spectroskopischen Methoden
    • RODER, H. (1981). Mobilitat in Proteinen unter nativen und denaturierden Bedingungen: Untersuchung von Trypsin Inhibitoren mit spectroskopischen Methoden. Diss. ETH No. 6932.
    • (1981) Diss , Issue.6932
    • RODER, H.1
  • 168
    • 84976203851 scopus 로고
    • Kinetics and cooperativity of the solvent exchange of individual amide protons in BPTI
    • in the Press
    • RODER, H., WAGNER, G. & WUTHRICH, K. (1983). Kinetics and cooperativity of the solvent exchange of individual amide protons in BPTI. Biochim. biophys. Acta (in the Press).
    • (1983) Biochim. biophys. Acta
    • RODER, H.1    WAGNER, G.2    WUTHRICH, K.3
  • 169
    • 84975951611 scopus 로고
    • Exchange kinetics of individual amide protons in thermally unfolded BPTI
    • in the Press
    • RODER, H., WAGNER, G. & WUTHRICH, K. (1983). Exchange kinetics of individual amide protons in thermally unfolded BPTI. Biochim. biophys. Acta (in the Press).
    • (1983) Biochim. biophys. Acta
    • RODER, H.1    WAGNER, G.2    WUTHRICH, K.3
  • 170
    • 0018801332 scopus 로고
    • An experimental procedure for increasing the structural resolution of chemical hydrogen exchange measurements on proteins: application to ribonuclease S peptide
    • ROSA, J. J. & RICHARDS, F. M. (1979). An experimental procedure for increasing the structural resolution of chemical hydrogen exchange measurements on proteins: application to ribonuclease S peptide. J. molec. Biol. 133, 399–416.
    • (1979) J. molec. Biol. , vol.133 , pp. 399-416
    • ROSA, J.J.1    RICHARDS, F.M.2
  • 171
    • 0019872903 scopus 로고
    • Hydrogen exchange from identified regions of the S-protein component of ribonuclease as a function of temperature, pH and the binding of the S-peptide.
    • ROSA, J. J. & RICHARDS, F. M. (1981). Hydrogen exchange from identified regions of the S-protein component of ribonuclease as a function of temperature, pH and the binding of the S-peptide. J. molec. Biol. 145, 835–851.
    • (1981) J. molec. Biol. , vol.145 , pp. 835-851
    • ROSA, J.J.1    RICHARDS, F.M.2
  • 172
    • 0000420098 scopus 로고
    • Kinetics of proton transfer reactions in aqueous solution: rates of internally hydrogen-bonded systems
    • ROSE, M. C. & STUEHR, J. (1968). Kinetics of proton transfer reactions in aqueous solution: rates of internally hydrogen-bonded systems. J. Am. chem. Soc. 90, 7205–7209.
    • (1968) J. Am. chem. Soc. , vol.90 , pp. 7205-7209
    • ROSE, M.C.1    STUEHR, J.2
  • 173
    • 0014409928 scopus 로고
    • Studies of hydrogen exchange in proteins
    • The exchange kinetics of bovine carbonic anhydrase.
    • ROSENBERG, A. & CHAKRAVARTI, K. (1968). Studies of hydrogen exchange in proteins. 1. The exchange kinetics of bovine carbonic anhydrase. J. biol. Chem. 243, 5193 – 5201.
    • (1968) J. biol. Chem. , vol.243 , Issue.1 , pp. 5193-5201
    • ROSENBERG, A.1    CHAKRAVARTI, K.2
  • 174
    • 0014691275 scopus 로고
    • Studies of hydrogen exchange in proteins
    • The reversible thermal unfolding of chymotrypsinogen A as studied by exchange kinetics.
    • ROSENBERG, A. & ENBERG, J. (1969). Studies of hydrogen exchange in proteins. II. The reversible thermal unfolding of chymotrypsinogen A as studied by exchange kinetics. J. biol. Chem. 244, 6153–6159.
    • (1969) J. biol. Chem. , vol.244 , Issue.2 , pp. 6153-6159
    • ROSENBERG, A.1    ENBERG, J.2
  • 175
    • 0019832866 scopus 로고
    • Nuclear overhauser effect study and assignment of D stem and reverse-Hoogsteen base pair proton resonance in yeast tRNA Asp
    • ROY, S. & REDFIELD, A. G. (1981). Nuclear overhauser effect study and assignment of D stem and reverse-Hoogsteen base pair proton resonance in yeast tRNA Asp. Nucl. Acids Res. 9, 7073–7078.
    • (1981) Nucl. Acids Res. , vol.9 , pp. 7073-7078
    • ROY, S.1    REDFIELD, A.G.2
  • 178
    • 0000591693 scopus 로고
    • Room temperature phosphorescence and the dynamic aspects of protein structure
    • SAVIOTTI, M. L. & GALLEY, W. C. (1974). Room temperature phosphorescence and the dynamic aspects of protein structure. Proc. natn. Acad. Sci. U.S.A. 71 (10), 4154–4158.
    • (1974) Proc. natn. Acad. Sci. U.S.A. , vol.71 , Issue.10 , pp. 4154-4158
    • SAVIOTTI, M.L.1    GALLEY, W.C.2
  • 179
    • 0000580797 scopus 로고
    • Slow hydrogen-deuterium exchange in a non-alpha-helical polyamide
    • SCARPA, J. S., MUELLER, D. D. & KLOTZ, I. M. (1967). Slow hydrogen-deuterium exchange in a non-alpha-helical polyamide. J. Am. chem. Soc. 89, 6024–6030.
    • (1967) J. Am. chem. Soc. , vol.89 , pp. 6024-6030
    • SCARPA, J.S.1    MUELLER, D.D.2    KLOTZ, I.M.3
  • 180
    • 77049276418 scopus 로고
    • The stability of hydrogen bonded peptide structures in aqueous solution
    • SCHELLMAN, J. A. (1955). The stability of hydrogen bonded peptide structures in aqueous solution. Cr. Lab. Carlsberg (Ser. Chim.) 29, 230–259.
    • (1955) Cr. Lab. Carlsberg (Ser. Chim.) , vol.29 , pp. 230-259
    • SCHELLMAN, J.A.1
  • 181
    • 0017802519 scopus 로고
    • Solvent denaturation
    • SCHELLMAN, J. A. (1978). Solvent denaturation. Biopolymers 17, 1305 – 1322.
    • (1978) Biopolymers , vol.17 , pp. 1305-1322
    • SCHELLMAN, J.A.1
  • 182
    • 84975972150 scopus 로고
    • Protein hydration dependence of the amide hydrogen exchange of lysozyme
    • University of Arizona, Tucson
    • SCHINKLE, J. (1983). Protein hydration dependence of the amide hydrogen exchange of lysozyme. Ph.D. dissertation, University of Arizona, Tucson.
    • (1983) Ph.D. dissertation
    • SCHINKLE, J.1
  • 183
    • 0017118909 scopus 로고
    • Comparison of isotope labelling of purines in three specific transfer RNA’s
    • SCHOEMAKER, H. J. P., GAMBLE, R. C., BUDZIK, G. P. & SCHIMMEL, P. R. (1976). Comparison of isotope labelling of purines in three specific transfer RNA’s.Biochemistry 15, 2800–2809.
    • (1976) Biochemistry , vol.15 , pp. 2800-2809
    • SCHOEMAKER, H.J.P.1    GAMBLE, R.C.2    BUDZIK, G.P.3    SCHIMMEL, P.R.4
  • 184
    • 25744457735 scopus 로고
    • Real space refinement of neutron diffraction data from carbon monoxide sperm whale myoglobin.
    • SCHOENBORN, B. P., HANSON, J. C., DARLING, G. D. & NORVELL, J. C. (1978). Real space refinement of neutron diffraction data from carbon monoxide sperm whale myoglobin. Acta, crystallogr. 34 A (Suppl. 4), 65.
    • (1978) Acta, crystallogr. , vol.34 A , Issue.4 , pp. 65
    • SCHOENBORN, B.P.1    HANSON, J.C.2    DARLING, G.D.3    NORVELL, J.C.4
  • 185
    • 0017160469 scopus 로고
    • Concentration dependent hydrogen exchange kinetics of 3H-labeled S-peptide in ribonuclease S
    • SCHRIER, A. A. & BALDWIN, R. L. (1976). Concentration dependent hydrogen exchange kinetics of 3H-labeled S-peptide in ribonuclease S. J. molec. Biol. 105, 409–426.
    • (1976) J. molec. Biol. , vol.105 , pp. 409-426
    • SCHRIER, A.A.1    BALDWIN, R.L.2
  • 186
    • 0017749336 scopus 로고
    • Mechanism of dissociation of S-peptide from ribonuclease S
    • SCHRIER, A. A. & BALDWIN, R. L. (1977). Mechanism of dissociation of S-peptide from ribonuclease S. Biochemistry 16, 4203–4209.
    • (1977) Biochemistry , vol.16 , pp. 4203-4209
    • SCHRIER, A.A.1    BALDWIN, R.L.2
  • 188
    • 0014225139 scopus 로고
    • Kinetic properties and the electric field effect of the helix-coil transition of poly-benzyl-L-glutamate determined from dielectric relaxation measurements.
    • SCHWARTZ, G. & SEELIG, J. (1968). Kinetic properties and the electric field effect of the helix-coil transition of poly-benzyl-L-glutamate determined from dielectric relaxation measurements. Biopolymers 6, 1263–1277.
    • (1968) Biopolymers , vol.6 , pp. 1263-1277
    • SCHWARTZ, G.1    SEELIG, J.2
  • 189
    • 0019600356 scopus 로고
    • Rates of structural fluctuations of lysozyme in the range of thermal unfolding transition
    • SEGAWA, S., NAKAYAMA, M. & SAKANE, M. (1981). Rates of structural fluctuations of lysozyme in the range of thermal unfolding transition. Biopolymers 20, 1691–1705.
    • (1981) Biopolymers , vol.20 , pp. 1691-1705
    • SEGAWA, S.1    NAKAYAMA, M.2    SAKANE, M.3
  • 190
    • 84975965609 scopus 로고
    • Normal mode paths for hydrogen exchange in the peptide ferrichrome.
    • in the Press
    • SHERIDAN, R. P., LEVY, R. M. & ENGLANDER, S. W. (1983). Normal mode paths for hydrogen exchange in the peptide ferrichrome. Proc. natn. Acad. Sci. U.S.A. 80 (in the Press).
    • (1983) Proc. natn. Acad. Sci. U.S.A. , pp. 80
    • SHERIDAN, R.P.1    LEVY, R.M.2    ENGLANDER, S.W.3
  • 191
    • 0016207302 scopus 로고
    • Electrostatic effects in myoglobin
    • Hydrogen ion equilibria in sperm whale ferrimyglobin
    • SHIRE, S. J., HANANIA, G. I. H. & GURD, F. R. N. (1974). Electrostatic effects in myoglobin. Hydrogen ion equilibria in sperm whale ferrimyglobin. Biochemistry 13, 2967–2974.
    • (1974) Biochemistry , vol.13 , pp. 2967-2974
    • SHIRE, S.J.1    HANANIA, G.I.H.2    GURD, F.R.N.3
  • 192
    • 0018800867 scopus 로고
    • Dynamic information from protein crystallography: an analysis of temperature factors from refinement of the hen egg-white lysozyme structure
    • STERNBERG, M. J. E., GRACE, D. E. P. & PHILLIPS, D. C. (1979). Dynamic information from protein crystallography: an analysis of temperature factors from refinement of the hen egg-white lysozyme structure. J. molec. Biol, 130, 231–253.
    • (1979) J. molec. Biol , vol.130 , pp. 231-253
    • STERNBERG, M.J.E.1    GRACE, D.E.P.2    PHILLIPS, D.C.3
  • 193
    • 1642577341 scopus 로고
    • Hydrogen-deuterium exchange study of amino acids and proteins by 200–230 nm spectroscopy.
    • TAKAHASHI, T., NAKANISHI, M. & TSUBOI, M. (1978). Hydrogen-deuterium exchange study of amino acids and proteins by 200–230 nm spectroscopy. Bull, chem. Soc. Japan 51, 1988–1990.
    • (1978) Bull, chem. Soc. Japan , vol.51 , pp. 1988-1990
    • TAKAHASHI, T.1    NAKANISHI, M.2    TSUBOI, M.3
  • 194
    • 0017349738 scopus 로고
    • Structure of myoglobin refined at 210 A resolution
    • II. Structure of deoxymyoglobin from sperm whale.
    • TAKANO, T. (1977). Structure of myoglobin refined at 210 A resolution. II. Structure of deoxymyoglobin from sperm whale. J. molec. Biol, no, 569–584.
    • (1977) J. molec. Biol , pp. 569-584
    • TAKANO, T.1
  • 195
    • 0014364651 scopus 로고
    • Protein denaturation
    • TANFORD, C. (1968). Protein denaturation. Adv. Protein Chem. 23, 122–282.
    • (1968) Adv. Protein Chem. , vol.23 , pp. 122-282
    • TANFORD, C.1
  • 196
    • 0014718113 scopus 로고
    • Protein denaturation
    • TANFORD, C. (1970). Protein denaturation. Adv. Protein Chem. 24, 1–95.
    • (1970) Adv. Protein Chem. , vol.24 , pp. 1-95
    • TANFORD, C.1
  • 197
    • 33947468892 scopus 로고
    • Theory of protein titration curves
    • TANFORD, C. & KIRKWOOD, J. G. (1957). Theory of protein titration curves. J. Am. chem. Soc. 79, 5333–5339.
    • (1957) J. Am. chem. Soc. , vol.79 , pp. 5333-5339
    • TANFORD, C.1    KIRKWOOD, J.G.2
  • 198
    • 0016650587 scopus 로고
    • Open states in native polynucleotides
    • TEITELBAUM, H. & ENGLANDER, S. W. (1975). Open states in native polynucleotides. J. molec. Biol. 92, 55 – 92.
    • (1975) J. molec. Biol. , vol.92 , pp. 55-92
    • TEITELBAUM, H.1    ENGLANDER, S.W.2
  • 199
    • 0009483389 scopus 로고
    • Approximate treatment of the conformational characteristics of a cyclic nonapeptide, cyclolinopeptide A.
    • TONELLI, A. E. (1971). Approximate treatment of the conformational characteristics of a cyclic nonapeptide, cyclolinopeptide A. Proc. natn. Acad. Sci. U.S.A. 68, 1203–1207.
    • (1971) Proc. natn. Acad. Sci. U.S.A. , vol.68 , pp. 1203-1207
    • TONELLI, A.E.1
  • 200
    • 0018339239 scopus 로고
    • Overall and localized fluctuation in the structure of a protein molecule
    • TSUBOI, M. & NAKANISHI, M. (1979). Overall and localized fluctuation in the structure of a protein molecule. Adv. Biophys. 12, 101–130.
    • (1979) Adv. Biophys. , vol.12 , pp. 101-130
    • TSUBOI, M.1    NAKANISHI, M.2
  • 201
    • 0344437481 scopus 로고
    • A simple hydrogen exchange method for cross-linked protein crystals.
    • TUCHSEN, E. & OTTESEN, M. (1979). A simple hydrogen exchange method for cross-linked protein crystals. Carlsberg Res. Commun. 44, 1–10.
    • (1979) Carlsberg Res. Commun. , vol.44 , pp. 1-10
    • TUCHSEN, E.1    OTTESEN, M.2
  • 202
    • 0020480264 scopus 로고
    • Protein dynamics in solution and in a crystalline environment: a molecular dynamics study
    • VAN GUNSTEREN, W. F. & KARPLUS, M. (1982). Protein dynamics in solution and in a crystalline environment: a molecular dynamics study. Biochemistry 21, 2259–2274.
    • (1982) Biochemistry , vol.21 , pp. 2259-2274
    • VAN GUNSTEREN, W.F.1    KARPLUS, M.2
  • 203
    • 0015219007 scopus 로고
    • The conformational properties of the basic pancreatic trypsin inhibitor
    • VINCENT, J., CHICHEPORTICHE, R. & LAZDUNSKI, M. (1971). The conformational properties of the basic pancreatic trypsin inhibitor. Eur. J. Biochem. 23, 401 – 411.
    • (1971) Eur. J. Biochem. , vol.23 , pp. 401-411
    • VINCENT, J.1    CHICHEPORTICHE, R.2    LAZDUNSKI, M.3
  • 204
    • 0017598170 scopus 로고
    • Nuclear magnetic resonance studies of exchangeable protons
    • II. The solvent exchange rate of the indole nitrogen proton of tryptophan derivatives.
    • WAELDER, S. F. & REDFIELD, A. G. (1977). Nuclear magnetic resonance studies of exchangeable protons. II. The solvent exchange rate of the indole nitrogen proton of tryptophan derivatives. Biopolymers 16, 623–629.
    • (1977) Biopolymers , vol.16 , pp. 623-629
    • WAELDER, S.F.1    REDFIELD, A.G.2
  • 205
    • 0019334807 scopus 로고
    • A novel application of nuclear overhauser enhancement in proteins: analysis of correlated events in the exchange of internal labile protons.
    • WAGNER, G. (1980). A novel application of nuclear overhauser enhancement in proteins: analysis of correlated events in the exchange of internal labile protons. Biochem biophys Res. Commun. 97, 614.
    • (1980) Biochem biophys Res. Commun. , vol.97 , pp. 614
    • WAGNER, G.1
  • 206
    • 0007935308 scopus 로고
    • Internal mobility in globular proteins
    • WAGNER, G. (1982). Internal mobility in globular proteins. Comments Molec. Cell. Biophysics 1, 261–280.
    • (1982) Comments Molec. Cell. Biophysics , vol.1 , pp. 261-280
    • WAGNER, G.1
  • 207
    • 0020711969 scopus 로고
    • Characterization of the distribution of internal motions in BPTI using a large number of internal NMR probes
    • WAGNER, G. (1983). Characterization of the distribution of internal motions in BPTI using a large number of internal NMR probes. Q. Rev. Biophys. 16, 1–87.
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 1-87
    • WAGNER, G.1
  • 208
    • 0017314060 scopus 로고
    • Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI)
    • ‘H-NMR studies, Biophys.
    • WAGNER, G., DEMARCO, A. & wüthrich, K. (1976). Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI). I. ‘H-NMR studies, Biophys. Struct. & Mechanism 2, 139–158.
    • (1976) Struct. & Mechanism , vol.2 , Issue.1 , pp. 139-158
    • WAGNER, G.1    DEMARCO, A.2    wüthrich, K.3
  • 209
    • 0020483829 scopus 로고
    • Amide proton exchange and surface conformation of the basic pancreatic trypsin inhibitor (BPTI) in solution: studies with two dimensional NMR
    • WAGNER, G. & WüTHRICH, K. (1982). Amide proton exchange and surface conformation of the basic pancreatic trypsin inhibitor (BPTI) in solution: studies with two dimensional NMR. J. molec. Biol. 160, 343-36i.
    • (1982) J. molec. Biol. , vol.160 , pp. 343-36i
    • WAGNER, G.1    WüTHRICH, K.2
  • 210
    • 0018137537 scopus 로고
    • Dynamic model of globular protein conformations based on NMR studies in solution
    • WAGNER, G. & WUTHRICH, K. (1978). Dynamic model of globular protein conformations based on NMR studies in solution. Nature, Lond. 275, 247–248.
    • (1978) Nature, Lond. , vol.275 , pp. 247-248
    • WAGNER, G.1    WUTHRICH, K.2
  • 211
    • 0018782123 scopus 로고
    • Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor
    • WAGNER, G. & WüTHRICH, K. (1979a). Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor. J. molec. Biol. 130, 31–37.
    • (1979) J. molec. Biol. , vol.130 , pp. 31-37
    • WAGNER, G.1    WüTHRICH, K.2
  • 212
    • 0018792408 scopus 로고
    • Structural interpretation of the amide proton exchange in the basic pancreatic trypsin inhibitor and related proteins
    • WAGNER, G. & WüTHRICH, K. (1979b). Structural interpretation of the amide proton exchange in the basic pancreatic trypsin inhibitor and related proteins. J. molec. Biol. 134, 75–94.
    • (1979) J. molec. Biol. , vol.134 , pp. 75-94
    • WAGNER, G.1    WüTHRICH, K.2
  • 213
    • 0020483829 scopus 로고
    • Amide proton exchange and surface conformation of the basic pancreatic trypsin inhibitor (BPTI) in solution studies with two dimensional NMR
    • WAGNER, G. & WüTHRICH, K. (1982). Amide proton exchange and surface conformation of the basic pancreatic trypsin inhibitor (BPTI) in solution studies with two dimensional NMR. J. molec. Biol. 160, 343-36i.
    • (1982) J. molec. Biol. , vol.160 , pp. 343-36i
    • WAGNER, G.1    WüTHRICH, K.2
  • 214
    • 0015243882 scopus 로고
    • Helical complexes of poly(rl) with copolymers of poly(rC) containing I
    • WANG, A. C. & KALLENBACH, N. R. (1971). Helical complexes of poly(rl) with copolymers of poly(rC) containing I, A and U residues. J. molec. Biol. 62, 591–607.
    • (1971) A and U residues. J. molec. Biol. , vol.62 , pp. 591-607
    • WANG, A.C.1    KALLENBACH, N.R.2
  • 215
    • 0000467270 scopus 로고
    • Electrostatic basis of structure-function correlation in proteins
    • WARSHEL, A. (1981). Electrostatic basis of structure-function correlation in proteins. Acct chem. Res. 14, 284–290.
    • (1981) Acct chem. Res. , vol.14 , pp. 284-290
    • WARSHEL, A.1
  • 216
    • 0020473268 scopus 로고
    • Mechanisms of hydrogen exchange from nuclear magnetic resonance studies of individual tryptophan indole NH hydrogens in lysozyme
    • WEDIN, R. E., DELEPIERRE, M., DOBSON, C. M. & POULSEN, F. M. (1982). Mechanisms of hydrogen exchange from nuclear magnetic resonance studies of individual tryptophan indole NH hydrogens in lysozyme. Biochemistry 21, 1098–1103.
    • (1982) Biochemistry , vol.21 , pp. 1098-1103
    • WEDIN, R.E.1    DELEPIERRE, M.2    DOBSON, C.M.3    POULSEN, F.M.4
  • 217
    • 0016252718 scopus 로고
    • Hydrogen-tritium exchange in polypeptides.
    • Models of alpha-helical and beta conformations.
    • WELCH, W. H. JR. & FASMAN, G. D. (1974). Hydrogen-tritium exchange in polypeptides. Models of alpha-helical and beta conformations. Biochemistry 13, 2455–2466.
    • (1974) Biochemistry , vol.13 , pp. 2455-2466
    • WELCH, W.H.1    FASMAN, G.D.2
  • 218
    • 0020014461 scopus 로고
    • The role of protein fluctuations in enzyme action: a review.
    • WELCH, G. R., SOMOGYI, B. & DAMJANOVICH, S. (1982). The role of protein fluctuations in enzyme action: a review. Prog. Biophys. molec. Biol. 39, 109–146.
    • (1982) Prog. Biophys. molec. Biol. , vol.39 , pp. 109-146
    • WELCH, G.R.1    SOMOGYI, B.2    DAMJANOVICH, S.3
  • 219
    • 0020586169 scopus 로고
    • The structure of apamin in solution: 2D NMR study.
    • WEMMER, D. E. & KALLENBACH, N. R. (1983). The structure of apamin in solution: 2D NMR study. Biochemistry 22, 1901–1906.
    • (1983) Biochemistry , vol.22 , pp. 1901-1906
    • WEMMER, D.E.1    KALLENBACH, N.R.2
  • 220
    • 0016813130 scopus 로고
    • Binding kinetics of mercury (II) to polynucleotides
    • WILLIAMS, M. N. & CROTHERS, D. M. (1975). Binding kinetics of mercury (II) to polynucleotides. J. molec. Biol. 14, 1944–1951.
    • (1975) J. molec. Biol. , vol.14 , pp. 1944-1951
    • WILLIAMS, M.N.1    CROTHERS, D.M.2
  • 221
    • 0000498521 scopus 로고
    • Concentration dependence of the diffusion coefficient of a dimerizing protein: BPTI
    • WILLS, P. R. & GEORGALLS, Y. (1981). Concentration dependence of the diffusion coefficient of a dimerizing protein: BPTI. J. phys. Chem. 85 3978-3984
    • (1981) J. phys. Chem. , vol.85 , pp. 3978-3984
    • WILLS, P.R.1    GEORGALLS, Y.2
  • 222
    • 0015188846 scopus 로고
    • Hydrogen isotope exchange in the study of protein conformation
    • WILLUMSEN, L. (1971). Hydrogen isotope exchange in the study of protein conformation. C. r. Trav. Lab. Carlsberg 38, 223–295.
    • (1971) C. r. Trav. Lab. Carlsberg , vol.38 , pp. 223-295
    • WILLUMSEN, L.1
  • 223
    • 0004259377 scopus 로고
    • Hydrogen exchange in ribonuclease A: neutron diffraction study
    • WLODAWER, A. & SJOLLN, L. (1982). Hydrogen exchange in ribonuclease A: neutron diffraction study. Proc. natn. Acad. Sci. U.S.A. 79, 1418–1422.
    • (1982) Proc. natn. Acad. Sci. U.S.A. , vol.79 , pp. 1418-1422
    • WLODAWER, A.1    SJOLLN, L.2
  • 224
    • 84976203438 scopus 로고
    • Dynamic solvent accessibility in the soybean trypsin inhibitor-trypsin complex
    • WOODWARD, C. K. (1977). Dynamic solvent accessibility in the soybean trypsin inhibitor-trypsin complex. J. molec. Biol. 11, 509—515.
    • (1977) J. molec. Biol. , vol.11 , pp. 509-515
    • WOODWARD, C.K.1
  • 225
    • 0016651412 scopus 로고
    • Solvent accessibility in folded proteins: studies of hydrogen exchange in trypsin.
    • WOODWARD, C. K., ELLIS, L. M. & ROSENBERG, A. (1975). Solvent accessibility in folded proteins: studies of hydrogen exchange in trypsin. J. biol. Chem. 250, 432–439.
    • (1975) J. biol. Chem. , vol.250 , pp. 432-439
    • WOODWARD, C.K.1    ELLIS, L.M.2    ROSENBERG, A.3
  • 226
    • 0016606350 scopus 로고
    • The solvent dependence of hydrogen exchange kinetics of folded proteins
    • WOODWARD, C. K., ELLIS, L. M. & ROSENBERG, A. (1975). The solvent dependence of hydrogen exchange kinetics of folded proteins. J. Biol. Chem. 250, 440–444.
    • (1975) J. Biol. Chem. , vol.250 , pp. 440-444
    • WOODWARD, C.K.1    ELLIS, L.M.2    ROSENBERG, A.3
  • 227
    • 0018368695 scopus 로고
    • Hydrogen exchange kinetics and internal motions in proteins and nucleic acids
    • WOODWARD, C. K. & HILTON, B. D. (1979). Hydrogen exchange kinetics and internal motions in proteins and nucleic acids. A. Rev. Biophys. Bioengng 8, 99–127.
    • (1979) A. Rev. Biophys. Bioengng , vol.8 , pp. 99-127
    • WOODWARD, C.K.1    HILTON, B.D.2
  • 228
    • 0019076960 scopus 로고
    • Hydrogen isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor
    • WOODWARD, C. K. & HILTON, B. D. (1980). Hydrogen isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor. Biophys. J. 32, 561-575
    • (1980) Biophys. J. , vol.32 , pp. 561-575
    • WOODWARD, C.K.1    HILTON, B.D.2
  • 229
    • 0014832199 scopus 로고
    • Oxidized RNase as a protein model having no contribution to the hydrogen exchange rate from conformational restrictions
    • WOODWARD, C. K. & ROSENBERG, A. (1970). Oxidized RNase as a protein model having no contribution to the hydrogen exchange rate from conformational restrictions. Proc. natn. Acad. Sci. U.S.A. 66, 1067—1074.
    • (1970) Proc. natn. Acad. Sci. U.S.A. , vol.66 , pp. 1067-1074
    • WOODWARD, C.K.1    ROSENBERG, A.2
  • 230
    • 0015218157 scopus 로고
    • Urea effects on hydrogen exchange kinetics leading to a general model for hydrogen exchange from folded proteins
    • WOODWARD, C. K. & ROSENBERG, A. (1971). Urea effects on hydrogen exchange kinetics leading to a general model for hydrogen exchange from folded proteins. J. biol. Chem. 246, 4114–4121.
    • (1971) J. biol. Chem. , vol.246 , pp. 4114-4121
    • WOODWARD, C.K.1    ROSENBERG, A.2
  • 231
    • 0015218075 scopus 로고
    • The correlation of ribonuclease exchange kinetics with the temperature induced transition.
    • WOODWARD, C. K. & ROSENBERG, A. (1971). The correlation of ribonuclease exchange kinetics with the temperature induced transition. J. biol. Chem. 246, 4105–4113.
    • (1971) J. biol. Chem. , vol.246 , pp. 4105-4113
    • WOODWARD, C.K.1    ROSENBERG, A.2
  • 232
    • 0020493395 scopus 로고
    • Hydrogen exchange and the dynamic structure of proteins.
    • WOODWARD, C. K., SIMON, I. & TUCHSEN, E. (1982). Hydrogen exchange and the dynamic structure of proteins. Mol. & Cell. Biochem. 48, 135 – 160.
    • (1982) Mol. & Cell. Biochem. , vol.48 , pp. 135-160
    • WOODWARD, C.K.1    SIMON, I.2    TUCHSEN, E.3
  • 233
    • 77956869116 scopus 로고
    • Internal mobility and unfolding of globular proteins.
    • (ed. R. Jaenicke)
    • WüTHRICH, K., röder, H. & WAGNER, G. (1980). Internal mobility and unfolding of globular proteins. In Protein Folding (ed. R. Jaenicke), PP- 549“564.
    • (1980) Protein Folding , pp. 549-564
    • WüTHRICH, K.1    röder, H.2    WAGNER, G.3
  • 234
    • 0018782084 scopus 로고
    • Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor
    • WÜTHRICH, K. & WAGNER, G. (1979). Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor. J. molec. Biol. 130, 1–18.
    • (1979) J. molec. Biol. , vol.130 , pp. 1-18
    • WÜTHRICH, K.1    WAGNER, G.2
  • 235
    • 84976203867 scopus 로고
    • A dynamic model for globular protein conformations based on high resolution NMR data.
    • Proceedings of the 12th FEBS Meeting, Dresden
    • WÜTHRICH, K., WAGNER, G. & RICHARZ, R. (1978). A dynamic model for globular protein conformations based on high resolution NMR data. In Protein: Structure, Function and Industrial Applications, Proceedings of the 12th FEBS Meeting, Dresden 1978
    • (1978) Protein: Structure, Function and Industrial Applications
    • WÜTHRICH, K.1    WAGNER, G.2    RICHARZ, R.3
  • 236
    • 0019077210 scopus 로고
    • Correlations between internal mobility and stability of globular proteins
    • WÜTHRICH, K., WAGNER, G., RICHARZ, R. & BRAUN, W. (1980). Correlations between internal mobility and stability of globular proteins. Biophys. J. 32, 549–560.
    • (1980) Biophys. J. , vol.32 , pp. 549-560
    • WÜTHRICH, K.1    WAGNER, G.2    RICHARZ, R.3    BRAUN, W.4
  • 237
    • 0014961294 scopus 로고
    • The 3-dimensional structuring of ribonuclease S
    • Interpretation of an electron density map at nominal resolution of 2 Å
    • WYCKOFF, H. W., TSERNOGLOU, D., HANSON, D., KNOX, J. R., LEE, B. & RICHARDS, F. M. (1970). The 3-dimensional structuring of ribonuclease S. Interpretation of an electron density map at nominal resolution of 2 Å. J. biol. Chem. 245, 305–328.
    • (1970) J. biol. Chem. , vol.245 , pp. 305-328
    • WYCKOFF, H.W.1    TSERNOGLOU, D.2    HANSON, D.3    KNOX, J.R.4    LEE, B.5    RICHARDS, F.M.6
  • 238
    • 67650040559 scopus 로고
    • Linked functions and reciprocal effects in hemoglobin: a second look
    • WYMAN, J. J. (1964). Linked functions and reciprocal effects in hemoglobin: a second look. Adv. Protein Chem. 19, 223–286.
    • (1964) Adv. Protein Chem. , vol.19 , pp. 223-286
    • WYMAN, J.J.1
  • 240
    • 84976147681 scopus 로고
    • Secondary structure in polyuridylic acid
    • YOUNG, P. R. & KALLENBACH, N. R. (1978). Secondary structure in polyuridylic acid. J. molec. Biol. 166, 467–479.
    • (1978) J. molec. Biol. , vol.166 , pp. 467-479
    • YOUNG, P.R.1    KALLENBACH, N.R.2
  • 241
    • 0014022717 scopus 로고
    • Ferrichrome A tetrahydrate
    • Determination of crystal and molecular structure.
    • ZALKIN, A., FORRESTER, J. D. & TEMPLETON, D. H. (1966). Ferrichrome A tetrahydrate. Determination of crystal and molecular structure. J. Am. chem. Soc. 88, 1810—1814.
    • (1966) J. Am. chem. Soc. , vol.88 , pp. 1810-1814
    • ZALKIN, A.1    FORRESTER, J.D.2    TEMPLETON, D.H.3
  • 242
    • 0000754002 scopus 로고
    • Theory of melting of chains of the helical form in double chains of the DNA type.
    • ZIMM, B. H. (1960). Theory of melting of chains of the helical form in double chains of the DNA type. J. chem. Phys. 33, 1349–1356.
    • (1960) J. chem. Phys. , vol.33 , pp. 1349-1356
    • ZIMM, B.H.1
  • 243
    • 0000668407 scopus 로고
    • Theory of the phase transition between helix and random coil in polypeptide chains
    • ZIMM, B. H. & BRAGG, J. K. (1959). Theory of the phase transition between helix and random coil in polypeptide chains. J. chem. Phys. 31, 526-535.
    • (1959) J. chem. Phys. , vol.31 , pp. 526-535
    • ZIMM, B.H.1    BRAGG, J.K.2
  • 244
    • 0015820466 scopus 로고
    • Pressure denaturation of metmyoglobin.
    • ZIPP, A. & KAUZMANN, W. (1973). Pressure denaturation of metmyoglobin. Biochemistry 12, 4217—4228.
    • (1973) Biochemistry , vol.12 , pp. 4217-4228
    • ZIPP, A.1    KAUZMANN, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.