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Volumn 66, Issue 2, 1996, Pages 167-196

Protein conformational substates from X-ray crystallography

Author keywords

[No Author keywords available]

Indexed keywords

ACTINIDIN; AZURIN; CHYMOTRYPSIN; ERABUTOXIN; FK 506 BINDING PROTEIN; HEMOGLOBIN; INSULIN; LIGAND; LYSOZYME; PROTEIN; PROTEINASE; RIBONUCLEASE A; SOLVENT;

EID: 0030435203     PISSN: 00796107     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0079-6107(97)85629-5     Document Type: Review
Times cited : (41)

References (175)
  • 1
    • 0026775898 scopus 로고
    • Charged surface residues of FKBP12 participate in formation of the FKBP12-FK506-calcineurin complex
    • Aldape, R. A., Futer, O., DeCenzo, M. T., Jarrett, B. P., Murcko, M. A. and Livingston, D. J. (1992) Charged surface residues of FKBP12 participate in formation of the FKBP12-FK506-calcineurin complex. J. biol. Chem. 267, 16029-16032.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16029-16032
    • Aldape, R.A.1    Futer, O.2    Decenzo, M.T.3    Jarrett, B.P.4    Murcko, M.A.5    Livingston, D.J.6
  • 3
    • 16044375105 scopus 로고
    • Crystal structures of HIV-1 protease-inhibitor complexes
    • Appelt, K. (1993) Crystal structures of HIV-1 protease-inhibitor complexes. Perspect. Drug Disc. Design 1, 23-48.
    • (1993) Perspect. Drug Disc. Design , vol.1 , pp. 23-48
    • Appelt, K.1
  • 11
    • 0028774339 scopus 로고
    • Influenza hemagglutinin: Kinetic control of protein function
    • Baker, D. and Agard, D. A. (1994) Influenza hemagglutinin: Kinetic control of protein function. Structure 2, 907-910.
    • (1994) Structure , vol.2 , pp. 907-910
    • Baker, D.1    Agard, D.A.2
  • 12
    • 0019156319 scopus 로고
    • Structure of actinidin, after refinement at 1.7 Å resolution
    • Baker, E. N. (1980) Structure of actinidin, after refinement at 1.7 Å resolution. J. molec. Biol. 141, 441-484.
    • (1980) J. Molec. Biol. , vol.141 , pp. 441-484
    • Baker, E.N.1
  • 15
    • 0013852463 scopus 로고
    • Structure of hen egg-white lysozyme: A three-dimensional Fourier synthesis at 2.0 Å resolution
    • Blake, C. C. F., Koenig, D. F., Mair, G. A., North, A. C. T., Phillips, D. C. and Sarma, V. R. (1965) Structure of hen egg-white lysozyme: A three-dimensional Fourier synthesis at 2.0 Å resolution. Nature 206, 757-761.
    • (1965) Nature , vol.206 , pp. 757-761
    • Blake, C.C.F.1    Koenig, D.F.2    Mair, G.A.3    North, A.C.T.4    Phillips, D.C.5    Sarma, V.R.6
  • 16
    • 0001510472 scopus 로고
    • The treatment of errors in the isomorphous replacement method
    • Blow, D. M. and Crick, F. H. C. (1959) The treatment of errors in the isomorphous replacement method. Acta Cryst. 12, 794-802.
    • (1959) Acta Cryst. , vol.12 , pp. 794-802
    • Blow, D.M.1    Crick, F.H.C.2
  • 17
    • 0030574268 scopus 로고    scopus 로고
    • Structure-based drug design
    • Blundell, T. L. (1996) Structure-based drug design. Nature (Suppl.) 384, 23-26.
    • (1996) Nature (Suppl.) , vol.384 , pp. 23-26
    • Blundell, T.L.1
  • 18
    • 0020441466 scopus 로고
    • Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate
    • Bolin, J. T., Filman, D. J., Matthews, D. A., Hamlin, R. C. and Kraut, J. (1982) Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate. J. biol. Chem. 257, 13,650-13,662.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13650-13662
    • Bolin, J.T.1    Filman, D.J.2    Matthews, D.A.3    Hamlin, R.C.4    Kraut, J.5
  • 19
    • 0029022355 scopus 로고
    • Conformational variability of solution nuclear magnetic resonance structures
    • Bonvin, A. M. and Brünger, A. T. (1995) Conformational variability of solution nuclear magnetic resonance structures. J. molec. Biol. 250, 80-93.
    • (1995) J. Molec. Biol. , vol.250 , pp. 80-93
    • Bonvin, A.M.1    Brünger, A.T.2
  • 20
    • 0029693351 scopus 로고    scopus 로고
    • Do NOE distances contain enough information to assess the relative populations of multi-conformer structures?
    • Bonvin, A. M. and Brünger, A. T. (1996) Do NOE distances contain enough information to assess the relative populations of multi-conformer structures? J. biomolec. NMR 7, 72-76.
    • (1996) J. Biomolec. NMR , vol.7 , pp. 72-76
    • Bonvin, A.M.1    Brünger, A.T.2
  • 21
  • 23
    • 0024279342 scopus 로고
    • Crystallographic refinement by simulated annealing. Application to a 2.8 Å resolution structure of aspartate aminotransferase
    • Brünger, A. T. (1988) Crystallographic refinement by simulated annealing. Application to a 2.8 Å resolution structure of aspartate aminotransferase. J. molec. Biol. 203, 803-816.
    • (1988) J. Molec. Biol. , vol.203 , pp. 803-816
    • Brünger, A.T.1
  • 24
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. (1992a) Free R value: A novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 26
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation: The free R value, methods and applications
    • Brünger, A. T. (1993) Assessment of phase accuracy by cross validation: The free R value, methods and applications. Acta Cryst. D49, 24-36.
    • (1993) Acta Cryst. , vol.D49 , pp. 24-36
    • Brünger, A.T.1
  • 27
    • 0029686650 scopus 로고    scopus 로고
    • Recent developments for crystallographic refinement of macromolecules
    • Brünger, A. T. (1996) Recent developments for crystallographic refinement of macromolecules. Meths molec. Biol. 56, 245-266.
    • (1996) Meths Molec. Biol. , vol.56 , pp. 245-266
    • Brünger, A.T.1
  • 28
    • 0027293559 scopus 로고
    • Computational challenges for macromolecular structure determination by X-ray crystallography and solution NMR-spectroscopy
    • Brünger, A. T. and Nilges, M. (1993) Computational challenges for macromolecular structure determination by X-ray crystallography and solution NMR-spectroscopy. Q. Rev. Biophys. 26, 49-125.
    • (1993) Q. Rev. Biophys. , vol.26 , pp. 49-125
    • Brünger, A.T.1    Nilges, M.2
  • 29
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson, J. D., Onuchic, J. N., Socci, N. D. and Wolynes, P. G. (1995) Funnels, pathways, and the energy landscape of protein folding: A synthesis. Proteins 21, 167-195.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 30
    • 0023449962 scopus 로고
    • Spin glasses and the statistical mechanics of protein folding
    • Bryngelson, J. D. and Wolynes, P. G. (1987) Spin glasses and the statistical mechanics of protein folding. Proc. natn. Acad. Sci. U.S.A. 84, 7524-7528.
    • (1987) Proc. Natn. Acad. Sci. U.S.A. , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 32
    • 85005537029 scopus 로고
    • Thermal motion and conformational disorder in protein crystal structures - Comparison of multi-conformer and time-averaging models
    • Burling, F. T. and Brünger, A. T. (1994) Thermal motion and conformational disorder in protein crystal structures - comparison of multi-conformer and time-averaging models. Israel J. Chem. 34, 165-175.
    • (1994) Israel J. Chem. , vol.34 , pp. 165-175
    • Burling, F.T.1    Brünger, A.T.2
  • 33
    • 0030038545 scopus 로고    scopus 로고
    • Direct observation of protein solvation and discrete disorder with experimental crystallographic phases
    • Burling, F. T., Weis, W. I., Flaherty, K. M. and Brünger, A. T. (1996) Direct observation of protein solvation and discrete disorder with experimental crystallographic phases. Science 271, 72-77.
    • (1996) Science , vol.271 , pp. 72-77
    • Burling, F.T.1    Weis, W.I.2    Flaherty, K.M.3    Brünger, A.T.4
  • 34
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C. M. and Kim, P. S. (1993) A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73, 823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 35
    • 36449000646 scopus 로고
    • Transition states and folding dynamics of proteins and heteropolymers
    • Chan, H. S. and Dill, K. A. (1994) Transition states and folding dynamics of proteins and heteropolymers. J. chem. Phys. 100, 9238-9257.
    • (1994) J. Chem. Phys. , vol.100 , pp. 9238-9257
    • Chan, H.S.1    Dill, K.A.2
  • 36
    • 0026551529 scopus 로고
    • Refinement of an enzyme complex with inhibitor bound at partial occupancy. Hen egg-white lysozyme and tri-N-acetylchitotriose at 1.75 Å resolution
    • Cheetham, J. C., Artymiuk, P. J. and Phillips, D. C. (1992) Refinement of an enzyme complex with inhibitor bound at partial occupancy. Hen egg-white lysozyme and tri-N-acetylchitotriose at 1.75 Å resolution. J. molec. Biol. 224, 613-628.
    • (1992) J. Molec. Biol. , vol.224 , pp. 613-628
    • Cheetham, J.C.1    Artymiuk, P.J.2    Phillips, D.C.3
  • 37
    • 0028078188 scopus 로고
    • Cross-validation tests of time-averaged molecular dynamics refinements for determination of protein structures by X-ray crystallography
    • Clarage, J. B. and Phillips, G. N. Jr. (1994) Cross-validation tests of time-averaged molecular dynamics refinements for determination of protein structures by X-ray crystallography. Acta Cryst. D50, 24-36.
    • (1994) Acta Cryst. , vol.D50 , pp. 24-36
    • Clarage, J.B.1    Phillips G.N., Jr.2
  • 38
    • 0021914675 scopus 로고
    • Kinetics of carbon monoxide binding to monomeric hemoproteins. Role of the proximal histidine
    • Coletta, M., Ascenzi, P., Traylor, T. G. and Brunori, M. (1985) Kinetics of carbon monoxide binding to monomeric hemoproteins. Role of the proximal histidine. J. biol. Chem. 260, 4151-4155.
    • (1985) J. Biol. Chem. , vol.260 , pp. 4151-4155
    • Coletta, M.1    Ascenzi, P.2    Traylor, T.G.3    Brunori, M.4
  • 39
    • 0028958868 scopus 로고
    • Flap opening in HIV-1 protease simulated by 'activated' molecular dynamics
    • Collins, J. R., Burt, S. K. and Erickson, J. W. (1995) Flap opening in HIV-1 protease simulated by 'activated' molecular dynamics. Nature struct. Biol. 2, 334-338.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 334-338
    • Collins, J.R.1    Burt, S.K.2    Erickson, J.W.3
  • 42
    • 0025756173 scopus 로고
    • Structure of γ-chymotrypsin in the range pH 2.0 to pH 10.5 suggests that γ-chymotrypsin is a covalent acyl-enzyme adduct at low pH
    • Dixon, M. M., Brennan, R. G. and Matthews, B. W. (1991) Structure of γ-chymotrypsin in the range pH 2.0 to pH 10.5 suggests that γ-chymotrypsin is a covalent acyl-enzyme adduct at low pH. Int. J. biol. Macromol. 13, 89-96.
    • (1991) Int. J. Biol. Macromol. , vol.13 , pp. 89-96
    • Dixon, M.M.1    Brennan, R.G.2    Matthews, B.W.3
  • 43
    • 0026802277 scopus 로고
    • Structure of a hingebending bacteriophage T4 lysozyme mutant, Ile3→Pro
    • Dixon, M. M., Nicholson, H., Shewchuk, L., Baase, W. A. and Matthews, B. W. (1992) Structure of a hingebending bacteriophage T4 lysozyme mutant, Ile3→Pro. J. molec. Biol. 227, 917-933.
    • (1992) J. Molec. Biol. , vol.227 , pp. 917-933
    • Dixon, M.M.1    Nicholson, H.2    Shewchuk, L.3    Baase, W.A.4    Matthews, B.W.5
  • 44
    • 0026740792 scopus 로고
    • Structural effects induced by mutagenesis affected by crystal packing factors: The structure of a 30-51 disulfide mutant of basic pancreatic trypsin inhibitor
    • Eigenbrot, C., Randal, M. and Kossiakoff, A. A. (1992) Structural effects induced by mutagenesis affected by crystal packing factors: The structure of a 30-51 disulfide mutant of basic pancreatic trypsin inhibitor. Proteins 14, 75-87.
    • (1992) Proteins , vol.14 , pp. 75-87
    • Eigenbrot, C.1    Randal, M.2    Kossiakoff, A.A.3
  • 45
    • 0023140044 scopus 로고
    • Multiple conformational states of proteins: A molecular dynamics analysis of myoglobin
    • Elber, R. and Karplus, M. (1987) Multiple conformational states of proteins: A molecular dynamics analysis of myoglobin. Science 235, 318-321.
    • (1987) Science , vol.235 , pp. 318-321
    • Elber, R.1    Karplus, M.2
  • 49
    • 0018793861 scopus 로고
    • Temperature-dependent X-ray diffraction as a probe of protein structural dynamics
    • Frauenfelder, H., Petsko, G. A. and Tsernoglou, D. (1979) Temperature-dependent X-ray diffraction as a probe of protein structural dynamics. Nature 280, 558-563.
    • (1979) Nature , vol.280 , pp. 558-563
    • Frauenfelder, H.1    Petsko, G.A.2    Tsernoglou, D.3
  • 50
    • 0026320866 scopus 로고
    • The energy landscape and motions of proteins
    • Frauenfelder, H., Sugar, S. G. and Wolynes, P. G. (1991) The energy landscape and motions of proteins. Science 254, 1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sugar, S.G.2    Wolynes, P.G.3
  • 51
    • 0002237761 scopus 로고
    • Biomolecules: Where the physics of complexity and simplicity meet
    • Frauenfelder, H. and Wolynes, P. G. (1994) Biomolecules: Where the physics of complexity and simplicity meet. Physics Today 47, 58-64.
    • (1994) Physics Today , vol.47 , pp. 58-64
    • Frauenfelder, H.1    Wolynes, P.G.2
  • 52
    • 0029079643 scopus 로고
    • FK506 binding protein mutational analysis: Defining the surface residue contributions to stability of the calcineurin co-complex
    • Futer, O., Decenzo, M. T., Aidape, R. A. and Livingston, D. J. (1995) FK506 binding protein mutational analysis: Defining the surface residue contributions to stability of the calcineurin co-complex. J. biol. Chem. 270, 18,935-18,940.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18935-18940
    • Futer, O.1    Decenzo, M.T.2    Aidape, R.A.3    Livingston, D.J.4
  • 53
    • 0001595086 scopus 로고
    • Proteins and glasses: A relaxation study in the millikelvin range
    • Gafert, J., Pschierer, H. and Friedrich, J. (1995) Proteins and glasses: A relaxation study in the millikelvin range. Phys. Rev. Lett. 74, 3704-3707.
    • (1995) Phys. Rev. Lett. , vol.74 , pp. 3704-3707
    • Gafert, J.1    Pschierer, H.2    Friedrich, J.3
  • 54
    • 0000577041 scopus 로고
    • Large-amplitude nonlinear motions in proteins
    • Garcia, A. E. (1992) Large-amplitude nonlinear motions in proteins. Phys. Rev. Lett. 68, 2696-2699.
    • (1992) Phys. Rev. Lett. , vol.68 , pp. 2696-2699
    • Garcia, A.E.1
  • 55
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • Gerstein, M., Lesk, A. M. and Chothia, C. (1994) Structural mechanisms for domain movements in proteins. Biochemistry 33, 6739-6749.
    • (1994) Biochemistry , vol.33 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3
  • 56
    • 0000902576 scopus 로고
    • Structural basis of hierarchical multiple substates of a protein
    • Go, N. and Noguti, T. (1989) Structural basis of hierarchical multiple substates of a protein. Chem. Scripta 29A, 151-164.
    • (1989) Chem. Scripta , vol.29 A , pp. 151-164
    • Go, N.1    Noguti, T.2
  • 57
    • 0025173665 scopus 로고
    • Inclusion of thermal motion in crystallographic structures by restrained molecular dynamics
    • Gros, P., van Gunsteren, W. F. and Hol, W. G. (1990) Inclusion of thermal motion in crystallographic structures by restrained molecular dynamics. Science 249, 1149-1152.
    • (1990) Science , vol.249 , pp. 1149-1152
    • Gros, P.1    Van Gunsteren, W.F.2    Hol, W.G.3
  • 58
    • 0026620720 scopus 로고
    • Conformational changes in cubic insulin crystals in the pH range 7-11
    • Gursky, O., Badger, J., Youli, L. and Caspar, D. L. D. (1992) Conformational changes in cubic insulin crystals in the pH range 7-11. Biophys. J. 63, 1210-1220.
    • (1992) Biophys. J. , vol.63 , pp. 1210-1220
    • Gursky, O.1    Badger, J.2    Youli, L.3    Caspar, D.L.D.4
  • 59
    • 0023054012 scopus 로고
    • Crystal structure analyses of reduced (CuI) poplar plastocyanin at six pH values
    • Guss, J. M., Harrowell, P. R., Murata, M., Norris, V. A. and Freeman, H. C. (1986) Crystal structure analyses of reduced (CuI) poplar plastocyanin at six pH values. J. molec. Biol. 192, 361-387.
    • (1986) J. Molec. Biol. , vol.192 , pp. 361-387
    • Guss, J.M.1    Harrowell, P.R.2    Murata, M.3    Norris, V.A.4    Freeman, H.C.5
  • 60
    • 0019888621 scopus 로고
    • Real space refinement of neutron diffraction data from sperm whale carbonmonoxymyoglobin
    • Hanson, J. C. and Schoenborn, B. P. (1981) Real space refinement of neutron diffraction data from sperm whale carbonmonoxymyoglobin. J. molec. Biol. 153, 117-146.
    • (1981) J. Molec. Biol. , vol.153 , pp. 117-146
    • Hanson, J.C.1    Schoenborn, B.P.2
  • 61
    • 0028001872 scopus 로고
    • X-ray structure of a monoclinic form of hen egg-white lysozyme crystallized at 313 K. Comparison of two independent molecules
    • Harata, K. (1994) X-ray structure of a monoclinic form of hen egg-white lysozyme crystallized at 313 K. Comparison of two independent molecules. Acta Cryst. D50, 250-257.
    • (1994) Acta Cryst. , vol.D50 , pp. 250-257
    • Harata, K.1
  • 62
    • 0002429554 scopus 로고
    • The phase problem of X-ray crystallography
    • Hauptman, H. A. (1989) The phase problem of X-ray crystallography. Physics Today 42, 24-29.
    • (1989) Physics Today , vol.42 , pp. 24-29
    • Hauptman, H.A.1
  • 63
    • 0022333121 scopus 로고
    • Stereochemically restrained refinement of macromolecular structures
    • Hendrickson, W. A. (1985) Stereochemically restrained refinement of macromolecular structures. Meths Enzymol. 115, 252-270.
    • (1985) Meths Enzymol. , vol.115 , pp. 252-270
    • Hendrickson, W.A.1
  • 64
    • 0019450355 scopus 로고
    • Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur
    • Hendrickson, W. A. and Teeter, M. M. (1981) Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur. Nature 290, 107-113.
    • (1981) Nature , vol.290 , pp. 107-113
    • Hendrickson, W.A.1    Teeter, M.M.2
  • 65
    • 0028297538 scopus 로고
    • Crystalline mitochondrial aspartate aminotransferase exists in only two conformations
    • Hohenester, E. and Jansonius, J. N. (1994) Crystalline mitochondrial aspartate aminotransferase exists in only two conformations. J. molec. Biol. 236, 963-968.
    • (1994) J. Molec. Biol. , vol.236 , pp. 963-968
    • Hohenester, E.1    Jansonius, J.N.2
  • 67
    • 0021842605 scopus 로고
    • Refinement of a molecular model for lamprey hemoglobin from Petromyzon marinus
    • Honzatko, R. B., Hendrickson, W. A. and Love, W. E. (1985) Refinement of a molecular model for lamprey hemoglobin from Petromyzon marinus. J. molec. Biol. 184, 147-164.
    • (1985) J. Molec. Biol. , vol.184 , pp. 147-164
    • Honzatko, R.B.1    Hendrickson, W.A.2    Love, W.E.3
  • 69
    • 0023512803 scopus 로고
    • Anisotropy and anharmonicity of atomic fluctuations in proteins: Analysis of a molecular dynamics simulation
    • Ichiye, T. and Karplus, M. (1987) Anisotropy and anharmonicity of atomic fluctuations in proteins: Analysis of a molecular dynamics simulation. Proteins 2, 236-259.
    • (1987) Proteins , vol.2 , pp. 236-259
    • Ichiye, T.1    Karplus, M.2
  • 70
    • 0024276807 scopus 로고
    • Anisotropy and anharmonicity of atomic fluctuations in proteins: Implications for X-ray analysis
    • Ichiye, T. and Karplus, M. (1988) Anisotropy and anharmonicity of atomic fluctuations in proteins: Implications for X-ray analysis. Biochemistry 27, 3487-3497.
    • (1988) Biochemistry , vol.27 , pp. 3487-3497
    • Ichiye, T.1    Karplus, M.2
  • 71
    • 0022794053 scopus 로고
    • Structure and internal mobility of proteins: A molecular dynamics study of hen egg white lysozyme
    • Ichiye, T., Olafson, B. D., Swaminathan, S. and Karplus, M. (1986) Structure and internal mobility of proteins: A molecular dynamics study of hen egg white lysozyme. Biopolymers 25, 1909-1937.
    • (1986) Biopolymers , vol.25 , pp. 1909-1937
    • Ichiye, T.1    Olafson, B.D.2    Swaminathan, S.3    Karplus, M.4
  • 72
    • 0025281494 scopus 로고
    • Molecular interactions in protein crystals: Solvent accessible surface and stability
    • Islam, S. A. and Weaver, D. L. (1990) Molecular interactions in protein crystals: Solvent accessible surface and stability. Proteins 8, 1-5.
    • (1990) Proteins , vol.8 , pp. 1-5
    • Islam, S.A.1    Weaver, D.L.2
  • 73
    • 0028984844 scopus 로고
    • Conformation of FK506 in X-ray structures of its complexes with human recombinant FKBPI2 mutants
    • Itoh, S., Decenzo, M. T., Livingston, D. J., Pearlman, D. A. and Navia, M. A. (1995) Conformation of FK506 in X-ray structures of its complexes with human recombinant FKBPI2 mutants. Bioorg. med. Chem. Lett. 5, 1983-1988.
    • (1995) Bioorg. Med. Chem. Lett. , vol.5 , pp. 1983-1988
    • Itoh, S.1    Decenzo, M.T.2    Livingston, D.J.3    Pearlman, D.A.4    Navia, M.A.5
  • 74
    • 0028788067 scopus 로고
    • Structure comparison of native and mutant human recombinant FKBP12 complexes with the immunosuppressant drag FK506 (tacrolimus)
    • Itoh, S. and Navia, M. A. (1995) Structure comparison of native and mutant human recombinant FKBP12 complexes with the immunosuppressant drag FK506 (tacrolimus). Prot. Sci. 4, 2261-2268.
    • (1995) Prot. Sci. , vol.4 , pp. 2261-2268
    • Itoh, S.1    Navia, M.A.2
  • 75
    • 84918314491 scopus 로고
    • Refinement of large structures by simultaneous minimization of energy and R factor
    • Jack, A. and Levitt, M. (1978) Refinement of large structures by simultaneous minimization of energy and R factor. Acta Cryst. A34, 931-935.
    • (1978) Acta Cryst. , vol.A34 , pp. 931-935
    • Jack, A.1    Levitt, M.2
  • 76
    • 0028774179 scopus 로고
    • Comparison of three different crystal forms shows HIV-1 reverse transcriptase displays an internal swivel motion
    • Jäger, J., Smerdon, S. J., Wang, J., Boisvert, D. C. and Steitz, T. A. (1994) Comparison of three different crystal forms shows HIV-1 reverse transcriptase displays an internal swivel motion. Structure 2, 869-876.
    • (1994) Structure , vol.2 , pp. 869-876
    • Jäger, J.1    Smerdon, S.J.2    Wang, J.3    Boisvert, D.C.4    Steitz, T.A.5
  • 78
    • 0025294520 scopus 로고
    • Refinement of protein dynamic structure: Normal mode refinement
    • Kidera, A. and Go, N. (1990) Refinement of protein dynamic structure: Normal mode refinement. Proc. natn. Acad. Sci. U.S.A. 87, 3718-3722.
    • (1990) Proc. Natn. Acad. Sci. U.S.A. , vol.87 , pp. 3718-3722
    • Kidera, A.1    Go, N.2
  • 79
    • 0026717834 scopus 로고
    • Normal mode refinement: Crystallographic refinement of protein dynamic structure II. Application to human lysozyme
    • Kidera, A., Inaka, I. C., Matsushima, M. and Go, N. (1992) Normal mode refinement: Crystallographic refinement of protein dynamic structure II. Application to human lysozyme. J. molec. Biol. 225, 477-486.
    • (1992) J. Molec. Biol. , vol.225 , pp. 477-486
    • Kidera, A.1    Inaka, I.C.2    Matsushima, M.3    Go, N.4
  • 80
    • 0025162691 scopus 로고
    • Crystal structure of low humidity tetragonal lysozyme at 2.1 Å, resolution. Variability in hydration shell and its structural consequences
    • Kodandajjani, R., Suresh, C. G. and Vijayan, M. (1990) Crystal structure of low humidity tetragonal lysozyme at 2.1 Å, resolution. Variability in hydration shell and its structural consequences. J. biol. Chem. 265, 16,126-16,131.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16126-16131
    • Kodandajjani, R.1    Suresh, C.G.2    Vijayan, M.3
  • 81
    • 0023494755 scopus 로고
    • A molecular dynamics simulation of crystalline alpha-cyclodextrin hexahydrate
    • Koehler, J. E. H., Saenger, W. and van Gunsteren, W. F. (1987) A molecular dynamics simulation of crystalline alpha-cyclodextrin hexahydrate. Arch. Biochem. Biophys. 15, 197-210.
    • (1987) Arch. Biochem. Biophys. , vol.15 , pp. 197-210
    • Koehler, J.E.H.1    Saenger, W.2    Van Gunsteren, W.F.3
  • 82
    • 0026645602 scopus 로고
    • Variability of conformations at crystal contacts in BPTI represent true low-energy structures: Correspondence among lattice packing and molecular dynamics structures
    • Kossiakoff, A. A., Randal, M., Guenot, J. and Eigenbrot, C. (1992) Variability of conformations at crystal contacts in BPTI represent true low-energy structures: Correspondence among lattice packing and molecular dynamics structures. Proteins 14, 6574.
    • (1992) Proteins , vol.14 , pp. 6574
    • Kossiakoff, A.A.1    Randal, M.2    Guenot, J.3    Eigenbrot, C.4
  • 83
    • 0026244229 scopus 로고
    • MOLSCRIPT - A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT - a program to produce both detailed and schematic plots of protein structures. J. appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 84
    • 0025328145 scopus 로고
    • Temperature dependence of the structure and dynamics of myoglobin. A simulation approach
    • Kuczera, K., Kuriyan, J. and Karplus, M. (1990) Temperature dependence of the structure and dynamics of myoglobin. A simulation approach. J. molec. Biol. 213, 351-373.
    • (1990) J. Molec. Biol. , vol.213 , pp. 351-373
    • Kuczera, K.1    Kuriyan, J.2    Karplus, M.3
  • 85
    • 0023644307 scopus 로고
    • Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres
    • Kundrot, C. E. and Richards, F. M. (1987) Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres. J. molec. Biol 193, 157-170.
    • (1987) J. Molec. Biol , vol.193 , pp. 157-170
    • Kundrot, C.E.1    Richards, F.M.2
  • 86
    • 0026730489 scopus 로고
    • Structure-based strategies for drug design and discovery
    • Kuntz, I. D. (1992) Structure-based strategies for drug design and discovery. Science 257, 1078-1082.
    • (1992) Science , vol.257 , pp. 1078-1082
    • Kuntz, I.D.1
  • 87
    • 0025943869 scopus 로고
    • Exploration of disorder in protein structures by X-ray restrained molecular dynamics
    • Kuriyan, J., Ösapay, K., Burley, S. K., Br̈nger, A. T., Hendrickson, W. A. and Karplus, M. (1991) Exploration of disorder in protein structures by X-ray restrained molecular dynamics. Proteins 10, 340-358.
    • (1991) Proteins , vol.10 , pp. 340-358
    • Kuriyan, J.1    Ösapay, K.2    Burley, S.K.3    Br̈nger, A.T.4    Hendrickson, W.A.5    Karplus, M.6
  • 88
    • 0023053635 scopus 로고
    • Effect of anisotropy and anharmonicity on protein Crystallographic refinement. An evaluation by molecular dynamics
    • Kuriyan, J., Petsko, G. A., Levy, R. M. and Karplus, M. (1986a) Effect of anisotropy and anharmonicity on protein Crystallographic refinement. An evaluation by molecular dynamics. J. molec. Biol. 190, 227-254.
    • (1986) J. Molec. Biol. , vol.190 , pp. 227-254
    • Kuriyan, J.1    Petsko, G.A.2    Levy, R.M.3    Karplus, M.4
  • 89
    • 0025904209 scopus 로고
    • Rigid protein motion as a model for Crystallographic temperature factors
    • Kuriyan, J. and Weis, W. I. (1991) Rigid protein motion as a model for Crystallographic temperature factors. Proc. natn. Acad. Sci. U.S.A. 88, 2773-2777.
    • (1991) Proc. Natn. Acad. Sci. U.S.A. , vol.88 , pp. 2773-2777
    • Kuriyan, J.1    Weis, W.I.2
  • 90
    • 0023042853 scopus 로고
    • X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 Å resolution
    • Kuriyan, J., Wilz, S., Karplus, M. and Petsko, G. A. (1986b) X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 Å resolution. J. molec. Biol. 192, 133-154.
    • (1986) J. Molec. Biol. , vol.192 , pp. 133-154
    • Kuriyan, J.1    Wilz, S.2    Karplus, M.3    Petsko, G.A.4
  • 91
    • 0029087668 scopus 로고
    • Phe-46(CD4) orients the distal histidine for hydrogen bonding to bound ligands in sperm whale myoglobin
    • Lai, H. H., Li, T., Lyons, D. S., Phillips, G. N. Jr., Olson, J. S. and Gibson, Q. H. (1995) Phe-46(CD4) orients the distal histidine for hydrogen bonding to bound ligands in sperm whale myoglobin. Proteins 22, 322-339.
    • (1995) Proteins , vol.22 , pp. 322-339
    • Lai, H.H.1    Li, T.2    Lyons, D.S.3    Phillips G.N., Jr.4    Olson, J.S.5    Gibson, Q.H.6
  • 92
    • 0028168285 scopus 로고
    • Crystallographic studies of savinase, a subtilisin-like proteinase, at pH 10.5
    • Lange, G., Betzel, C., Branner, S. and Wilson, K. S. (1994) Crystallographic studies of savinase, a subtilisin-like proteinase, at pH 10.5. Eur. J. Biochem. 224, 507-518.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 507-518
    • Lange, G.1    Betzel, C.2    Branner, S.3    Wilson, K.S.4
  • 93
    • 0024281641 scopus 로고
    • Three-dimensional structure at 0.86 Å of the uncomplexed form of the transmembrane ion channel peptide gramicidin A
    • Langs, D. A. (1988) Three-dimensional structure at 0.86 Å of the uncomplexed form of the transmembrane ion channel peptide gramicidin A. Science 241, 188-191.
    • (1988) Science , vol.241 , pp. 188-191
    • Langs, D.A.1
  • 95
    • 0029951039 scopus 로고    scopus 로고
    • Why are protein crystallographic R-values so high?
    • Lattman, E. E. (1996) Why are protein Crystallographic R-values so high? Proteins 25, R1-R2.
    • (1996) Proteins , vol.25
    • Lattman, E.E.1
  • 96
    • 0029099219 scopus 로고
    • Looking into the energy lardscape of myoglobin
    • Leeson, D. T. and Wiersma, D. A. (1995) Looking into the energy lardscape of myoglobin. Nature struct. Biol. 2, 848-851.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 848-851
    • Leeson, D.T.1    Wiersma, D.A.2
  • 97
    • 0039139534 scopus 로고
    • Born-Oppenheimer energy surfaces of similar molecules: Interrelations between bond lengths, bond angles, and frequencies of normal vibrations in alkanes
    • Lifson, S. and Stern, P. S. (1982) Born-Oppenheimer energy surfaces of similar molecules: Interrelations between bond lengths, bond angles, and frequencies of normal vibrations in alkanes. J. chem. Phys. 77, 4542-4550.
    • (1982) J. Chem. Phys. , vol.77 , pp. 4542-4550
    • Lifson, S.1    Stern, P.S.2
  • 98
    • 0025091668 scopus 로고
    • Stereochemical mechanism of action for thymidylate synthase based on the X-ray structure of the covalent inhibitory ternary complex with 5-fluoro-2′-deoxyuridylate and 5,10-methylenetetrahydrofolate
    • Matthews, D. A., Villafranca, J. E., Janson, C. A., Smith, W. W., Welsh, K. and Freer, S. (1990) Stereochemical mechanism of action for thymidylate synthase based on the X-ray structure of the covalent inhibitory ternary complex with 5-fluoro-2′-deoxyuridylate and 5,10-methylenetetrahydrofolate. J. molec. Biol. 214, 937-948.
    • (1990) J. Molec. Biol. , vol.214 , pp. 937-948
    • Matthews, D.A.1    Villafranca, J.E.2    Janson, C.A.3    Smith, W.W.4    Welsh, K.5    Freer, S.6
  • 99
    • 0014214281 scopus 로고
    • Manifestation of the tertiary structures of proteins in high frequency nuclear magnetic resonance
    • McDonald, C. C. and Phillips, W. D. (1967) Manifestation of the tertiary structures of proteins in high frequency nuclear magnetic resonance. J. Am. Chem. Soc. 89, 6332-6341.
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 6332-6341
    • McDonald, C.C.1    Phillips, W.D.2
  • 100
    • 0026751404 scopus 로고
    • X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase
    • McPhalen, C. A., Vincent, M. G. and Jansonius, J. N. (1992) X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase. J. molec. Biol. 225, 495-517.
    • (1992) J. Molec. Biol. , vol.225 , pp. 495-517
    • McPhalen, C.A.1    Vincent, M.G.2    Jansonius, J.N.3
  • 101
    • 0029067489 scopus 로고
    • Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: Linkage of dynamics and structural plasticity
    • Morton, A. and Matthews, B. W. (1995) Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: Linkage of dynamics and structural plasticity. Biochemistry 34, 8576-8588.
    • (1995) Biochemistry , vol.34 , pp. 8576-8588
    • Morton, A.1    Matthews, B.W.2
  • 102
    • 0027506631 scopus 로고
    • Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop
    • Muller, C. W. and Schulz, G. E. (1993) Crystal structures of two mutants of adenylate kinase from Escherichia coli that modify the Gly-loop. Proteins 15, 42-49.
    • (1993) Proteins , vol.15 , pp. 42-49
    • Muller, C.W.1    Schulz, G.E.2
  • 103
    • 0030485289 scopus 로고    scopus 로고
    • An X-ray analysis of native monoclinic lysozyme. A case study on the reliability of refined protein structures and a comparison with the low-humidity form in relation to mobility and enzyme action
    • Nagendra, H. G., Sudarsanakumar, C. and Vijayan, M. (1996) An X-ray analysis of native monoclinic lysozyme. A case study on the reliability of refined protein structures and a comparison with the low-humidity form in relation to mobility and enzyme action. Acta Cryst. D52, 1067-1074.
    • (1996) Acta Cryst. , vol.D52 , pp. 1067-1074
    • Nagendra, H.G.1    Sudarsanakumar, C.2    Vijayan, M.3
  • 104
    • 0028566709 scopus 로고
    • A reassessment of the structure of chymotrypsin inhibitor 2 (CI-2) using time-averaged NMR restraints
    • Nanzer, A. P., Poulsen, F. M., van Gunsteren, W. F. and Torda, A. E. (1994) A reassessment of the structure of chymotrypsin inhibitor 2 (CI-2) using time-averaged NMR restraints. Biochemistry 33, 14,503-14,511.
    • (1994) Biochemistry , vol.33 , pp. 14503-14511
    • Nanzer, A.P.1    Poulsen, F.M.2    Van Gunsteren, W.F.3    Torda, A.E.4
  • 105
    • 0025953438 scopus 로고
    • Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip
    • Nar, H., Messerschmidt, A., Huber, R., van de Kamp, M. and Canters, G. W. (1991) Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip. J. molec. Biol. 221, 765-772.
    • (1991) J. Molec. Biol. , vol.221 , pp. 765-772
    • Nar, H.1    Messerschmidt, A.2    Huber, R.3    Van De Kamp, M.4    Canters, G.W.5
  • 107
    • 33845550595 scopus 로고
    • Energy parameters in polypeptides. IX. Updating of geometrical parameters, nonbonded interactions, and hydrogen bond interactions for the naturally occurring amino acids
    • Nemethy, G., Pottie, M. S. and Scheraga, H. A. (1983) Energy parameters in polypeptides. IX. Updating of geometrical parameters, nonbonded interactions, and hydrogen bond interactions for the naturally occurring amino acids. J. phys. Chem. 87, 1883-1887.
    • (1983) J. Phys. Chem. , vol.87 , pp. 1883-1887
    • Nemethy, G.1    Pottie, M.S.2    Scheraga, H.A.3
  • 109
    • 0027242141 scopus 로고
    • Structures of the "open" and "closed" state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: Implications for the reaction mechanism
    • Noble, M. E., Zeelen, J. P. and Wierenga, R. K. (1993) Structures of the "open" and "closed" state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: Implications for the reaction mechanism. Proteins 16, 311-326.
    • (1993) Proteins , vol.16 , pp. 311-326
    • Noble, M.E.1    Zeelen, J.P.2    Wierenga, R.K.3
  • 110
    • 0027235488 scopus 로고
    • Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand
    • Oh, B.H., Pandit, J., Kang, C. H., Nikaido, K., Gokcen, S., Ames, G. F. and Kim, S. H. (1993) Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand. J. biol. Chem. 268, 11,348-11,355.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11348-11355
    • Oh, B.H.1    Pandit, J.2    Kang, C.H.3    Nikaido, K.4    Gokcen, S.5    Ames, G.F.6    Kim, S.H.7
  • 111
    • 0027980862 scopus 로고
    • Polypeptide conformational space. Dynamics by solution NMR disorder by X-ray crystallography
    • Pascal, S. M. and Cross, T. A. (1994) Polypeptide conformational space. Dynamics by solution NMR disorder by X-ray crystallography. J. molec. Biol. 241, 431-439.
    • (1994) J. Molec. Biol. , vol.241 , pp. 431-439
    • Pascal, S.M.1    Cross, T.A.2
  • 112
    • 0025778738 scopus 로고
    • Are time-averaged restraints necessary for nuclear magnetic resonance refinement? A model study for DNA
    • Pearlman, D. A. and Kollman, P. A. (1991) Are time-averaged restraints necessary for nuclear magnetic resonance refinement? A model study for DNA. J. molec. Biol. 220, 457-479.
    • (1991) J. Molec. Biol. , vol.220 , pp. 457-479
    • Pearlman, D.A.1    Kollman, P.A.2
  • 113
    • 0029972976 scopus 로고    scopus 로고
    • Not just your average structures
    • Petsko, G. A. (1996) Not just your average structures. Nature struct. Biol. 3, 565-566.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 565-566
    • Petsko, G.A.1
  • 114
    • 0021191208 scopus 로고
    • Fluctuations in protein structure from X-ray diffraction
    • Petsko, G. A. and Ringe, D. (1984) Fluctuations in protein structure from X-ray diffraction. A. Rev. Biophys. Bioeng. 13, 331-371.
    • (1984) A. Rev. Biophys. Bioeng. , vol.13 , pp. 331-371
    • Petsko, G.A.1    Ringe, D.2
  • 115
    • 0025037796 scopus 로고
    • Comparison of the dynamics of myoglobin in different crystal forms
    • Phillips, G. N. Jr. (1990) Comparison of the dynamics of myoglobin in different crystal forms. Biophys. J. 57, 381-383.
    • (1990) Biophys. J. , vol.57 , pp. 381-383
    • Phillips G.N., Jr.1
  • 116
    • 0019209443 scopus 로고
    • Structure and refinement of oxymyoglobin at 1.6 Å resolution
    • Phillips, S. E. (1980) Structure and refinement of oxymyoglobin at 1.6 Å resolution. J. molec. Biol. 142, 531-554.
    • (1980) J. Molec. Biol. , vol.142 , pp. 531-554
    • Phillips, S.E.1
  • 117
    • 0028220369 scopus 로고
    • A structural basis for the interaction of urea with lysozyme
    • Pike, A. C. and Acharya, K. R. (1994) A structural basis for the interaction of urea with lysozyme. Prot. Sci. 3, 706-710.
    • (1994) Prot. Sci. , vol.3 , pp. 706-710
    • Pike, A.C.1    Acharya, K.R.2
  • 118
    • 0023042577 scopus 로고
    • Molecular dynamics simulations of native and substratebound lysozyme. A study of the average structures and atomic fluctuations
    • Post, C. B., Brooks, B. R., Karplus, M., Dobson, C. M., Artymiuk, P. J., Cheetham, J. C. and Phillips, D. C. (1986) Molecular dynamics simulations of native and substratebound lysozyme. A study of the average structures and atomic fluctuations. J. molec. Biol 190, 455-479.
    • (1986) J. Molec. Biol , vol.190 , pp. 455-479
    • Post, C.B.1    Brooks, B.R.2    Karplus, M.3    Dobson, C.M.4    Artymiuk, P.J.5    Cheetham, J.C.6    Phillips, D.C.7
  • 119
    • 0024406542 scopus 로고
    • A molecular dynamics analysis of protein structural elements
    • Post, C. B., Dobson, C. M. and Karplus, M. (1989) A molecular dynamics analysis of protein structural elements. Proteins 5, 337-354.
    • (1989) Proteins , vol.5 , pp. 337-354
    • Post, C.B.1    Dobson, C.M.2    Karplus, M.3
  • 120
    • 0027368854 scopus 로고
    • High resolution crystal structures of distal histidine mutants of sperm whale myoglobin
    • Quillin, M. L., Arduini, R. M., Olson, J. S. and Phillips, G. N. Jr. (1993) High resolution crystal structures of distal histidine mutants of sperm whale myoglobin. J. molec. Biol 234, 140-155.
    • (1993) J. Molec. Biol , vol.234 , pp. 140-155
    • Quillin, M.L.1    Arduini, R.M.2    Olson, J.S.3    Phillips G.N., Jr.4
  • 121
    • 0030020251 scopus 로고    scopus 로고
    • Studies of monoclinic hen egg-white lysozyme: IV. X-ray refinement at 1.8 Å resolution and a comparison of the variable regions in the polymorphic forms
    • Rao, S. T. and Sundaralingam, M. (1996) Studies of monoclinic hen egg-white lysozyme: IV. X-ray refinement at 1.8 Å resolution and a comparison of the variable regions in the polymorphic forms. Acta Cryst. D52, 170-175.
    • (1996) Acta Cryst. , vol.D52 , pp. 170-175
    • Rao, S.T.1    Sundaralingam, M.2
  • 122
    • 0011218635 scopus 로고
    • Protein conformational substates from X-ray crystallography
    • (eds. A. J. Kungl, P. J. Andrew and H. Schreiber), Gesellschaft Osterreichischer Chemiker, Vienna
    • Rejto, P. A. and Freer, S. T. (1995) Protein conformational substates from X-ray crystallography. In The International Conference on Molecular Structural Biology (eds. A. J. Kungl, P. J. Andrew and H. Schreiber), pp. 68, Gesellschaft Osterreichischer Chemiker, Vienna.
    • (1995) The International Conference on Molecular Structural Biology , pp. 68
    • Rejto, P.A.1    Freer, S.T.2
  • 123
    • 0022555901 scopus 로고
    • Study of protein dynamics by X-ray diffraction
    • Ringe, D. and Petsko, G. A. (1986) Study of protein dynamics by X-ray diffraction. Meths Enzymol. 131, 389-433.
    • (1986) Meths Enzymol. , vol.131 , pp. 389-433
    • Ringe, D.1    Petsko, G.A.2
  • 124
    • 0029113863 scopus 로고
    • Automatic identification of discrete substates in proteins: Singular value decomposition analysis of time-averaged crystallographic refinements
    • Romo, T. D., Clarage, J. B., Sorensen, D. C. and Phillips, G. N. Jr. (1995) Automatic identification of discrete substates in proteins: Singular value decomposition analysis of time-averaged crystallographic refinements. Proteins 22, 311-321.
    • (1995) Proteins , vol.22 , pp. 311-321
    • Romo, T.D.1    Clarage, J.B.2    Sorensen, D.C.3    Phillips G.N., Jr.4
  • 125
    • 0028174310 scopus 로고
    • How does a protein fold?
    • Sali, A., Shakhnovich, E. and Karplus, M. (1994a) How does a protein fold? Nature 369, 248-251.
    • (1994) Nature , vol.369 , pp. 248-251
    • Sali, A.1    Shakhnovich, E.2    Karplus, M.3
  • 126
    • 0028270634 scopus 로고
    • Kinetics of protein folding. A lattice model study of the requirements for folding to the native state
    • Sali, A., Shakhnovich, E. and Karplus, M. (1994b) Kinetics of protein folding. A lattice model study of the requirements for folding to the native state. J. molec. Biol. 235, 1614-1636.
    • (1994) J. Molec. Biol. , vol.235 , pp. 1614-1636
    • Sali, A.1    Shakhnovich, E.2    Karplus, M.3
  • 128
    • 0011181452 scopus 로고
    • Time-averaging crystallographic refinement: Possibilities and limitations using α-cyclodextrin as a test system
    • Schiffer, C. A., Gros, P. and Van Gunsteren, W. F. (1995) Time-averaging crystallographic refinement: Possibilities and limitations using α-cyclodextrin as a test system. Acta Cryst. D51, 85-92.
    • (1995) Acta Cryst. , vol.D51 , pp. 85-92
    • Schiffer, C.A.1    Gros, P.2    Van Gunsteren, W.F.3
  • 129
    • 0027983623 scopus 로고
    • Simultaneous refinement of the structure of BPTI against NMR data measured in solution and X-ray diffraction data measured in single crystals
    • Schiffer, C. A., Huber, R., Wüthrich, K. and van Gunsteren, W. F. (1994) Simultaneous refinement of the structure of BPTI against NMR data measured in solution and X-ray diffraction data measured in single crystals. J. molec. Biol 241, 588-599.
    • (1994) J. Molec. Biol , vol.241 , pp. 588-599
    • Schiffer, C.A.1    Huber, R.2    Wüthrich, K.3    Van Gunsteren, W.F.4
  • 130
  • 131
    • 0001841380 scopus 로고
    • On the rigid-body motion of molecules in crystals
    • Schomaker, V. and Trueblood, K. N. (1968) On the rigid-body motion of molecules in crystals. Acta Cryst. B24, 63-76.
    • (1968) Acta Cryst. , vol.B24 , pp. 63-76
    • Schomaker, V.1    Trueblood, K.N.2
  • 132
    • 0026493924 scopus 로고
    • Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis
    • Sharff, A. J., Rodseth, L. E., Spurlino, J. C. and Quiocho, F. A. (1992) Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis. Biochemistry 31, 10,657-10,663.
    • (1992) Biochemistry , vol.31 , pp. 10657-10663
    • Sharff, A.J.1    Rodseth, L.E.2    Spurlino, J.C.3    Quiocho, F.A.4
  • 133
    • 84943920736 scopus 로고
    • Phase annealing in Shelx-90 - Direct methods for larger structures
    • Sheldrick, G. M. (1990) Phase annealing in Shelx-90 - direct methods for larger structures. Acta Cryst. A46, 467-473.
    • (1990) Acta Cryst. , vol.A46 , pp. 467-473
    • Sheldrick, G.M.1
  • 137
    • 0007725036 scopus 로고
    • Folding kinetics of proteinlike heteropolymers
    • Socci, N. D. and Onuchic, J. N. (1994) Folding kinetics of proteinlike heteropolymers. J. chem. Phys. 101, 1519-1528.
    • (1994) J. Chem. Phys. , vol.101 , pp. 1519-1528
    • Socci, N.D.1    Onuchic, J.N.2
  • 138
    • 0026780442 scopus 로고
    • Substitution of Asp193 to Asn at the active site of ribulose-1,5-bisphosphate carboxylase results in conformational changes
    • Soderlind, E., Schneider, G. and Gutteridge, S. (1992) Substitution of Asp193 to Asn at the active site of ribulose-1,5-bisphosphate carboxylase results in conformational changes. Eur. J. Biochem. 206, 729-735.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 729-735
    • Soderlind, E.1    Schneider, G.2    Gutteridge, S.3
  • 139
    • 0025754301 scopus 로고
    • The 2.3 Å resolution structure of the maltose-or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
    • Spurlino, J. C., Lu, G.-Y. and Quiocho, F. A. (1991) The 2.3 Å resolution structure of the maltose-or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. biol. Chem. 266, 5202-5219.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5202-5219
    • Spurlino, J.C.1    Lu, G.-Y.2    Quiocho, F.A.3
  • 140
    • 0028887396 scopus 로고
    • Full-matrix refinement of the protein crambin at 0.83 Angstrom and 130 K
    • Stec, B., Zhou, R. and Teeter, M. M. (1995) Full-matrix refinement of the protein crambin at 0.83 Angstrom and 130 K. Acta Cryst. D51, 663-681.
    • (1995) Acta Cryst. , vol.D51 , pp. 663-681
    • Stec, B.1    Zhou, R.2    Teeter, M.M.3
  • 141
    • 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., Grace, D. E. and 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, 231-252.
    • (1979) J. Molec. Biol. , vol.130 , pp. 231-252
    • Sternberg, M.J.1    Grace, D.E.2    Phillips, D.C.3
  • 143
    • 0028786432 scopus 로고
    • Contribution of hydrophobic residues to the stability of human lysozyme: Calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants
    • Takano, K., Ogasahara, K., Kaneda, H., Yamagata, Y., Fujii, S., Kanaya, E., Kikuchi, M., Oobatake, M. and Yutani, K. (1995) Contribution of hydrophobic residues to the stability of human lysozyme: Calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants. J. molec. Biol. 254, 62-76.
    • (1995) J. Molec. Biol. , vol.254 , pp. 62-76
    • Takano, K.1    Ogasahara, K.2    Kaneda, H.3    Yamagata, Y.4    Fujii, S.5    Kanaya, E.6    Kikuchi, M.7    Oobatake, M.8    Yutani, K.9
  • 144
    • 0019881775 scopus 로고
    • Primary structure of the hydrophobic plant protein crambin
    • Teeter, M. M., Mazer, J. A. and L'Italien, J. J. (1981) Primary structure of the hydrophobic plant protein crambin. Biochemistry 20, 5437-5443.
    • (1981) Biochemistry , vol.20 , pp. 5437-5443
    • Teeter, M.M.1    Mazer, J.A.2    L'Italien, J.J.3
  • 145
    • 0027459475 scopus 로고
    • Atomic resolution (0.83 Å) crystal structure of the hydrophobic protein crambin at 130 K
    • Teeter, M. M., Roe, S. M. and Heo, N. H. (1993) Atomic resolution (0.83 Å) crystal structure of the hydrophobic protein crambin at 130 K. J. molec. Biol. 230, 292-311.
    • (1993) J. Molec. Biol. , vol.230 , pp. 292-311
    • Teeter, M.M.1    Roe, S.M.2    Heo, N.H.3
  • 146
    • 0028519126 scopus 로고
    • Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K
    • Teng, T. Y., Srajer, V. and Moffat, K. (1994) Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K. Nature struct. Biol. 1, 701-705.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 701-705
    • Teng, T.Y.1    Srajer, V.2    Moffat, K.3
  • 147
    • 0000437307 scopus 로고
    • Time-dependent distance restraints in molecular dynamics simulations
    • Torda, A. E., Scheek, R. M. and van Gunsteren, W. F. (1989) Time-dependent distance restraints in molecular dynamics simulations. Chem. Phys. Lett. 157, 289-294.
    • (1989) Chem. Phys. Lett. , vol.157 , pp. 289-294
    • Torda, A.E.1    Scheek, R.M.2    Van Gunsteren, W.F.3
  • 148
    • 0028338985 scopus 로고
    • Three-dimensional structure of endo-1,4-beta-xylanase II from Trichoderma reesei: Two conformational states in the active site
    • Torronen, A., Harkki, A. and Rouvinen, J. (1994) Three-dimensional structure of endo-1,4-beta-xylanase II from Trichoderma reesei: Two conformational states in the active site. Eur. molec. Biol. Org. J. 13, 2493-2501.
    • (1994) Eur. Molec. Biol. Org. J. , vol.13 , pp. 2493-2501
    • Torronen, A.1    Harkki, A.2    Rouvinen, J.3
  • 149
    • 0029152775 scopus 로고
    • Protein conformational landscapes: Energy minimization and clustering of a long molecular dynamics trajectory
    • Troyer, J. M. and Cohen, F. E. (1995) Protein conformational landscapes: Energy minimization and clustering of a long molecular dynamics trajectory. Proteins 23, 97-110.
    • (1995) Proteins , vol.23 , pp. 97-110
    • Troyer, J.M.1    Cohen, F.E.2
  • 150
    • 0025826967 scopus 로고
    • Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex
    • Van Duyne, G. D., Standaert, R. F., Karplus, P. A., Schreiber, S. L. and Clardy, J. (1991a) Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex. Science 252, 839-842.
    • (1991) Science , vol.252 , pp. 839-842
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 151
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with Fk506 and rapamycin
    • Van Duyne, G. D., Standaert, R. F., Karplus, P. A., Schreiber, S. L. and Clardy, J. (1993) Atomic structures of the human immunophilin FKBP-12 complexes with Fk506 and rapamycin. J. molec. Biol. 229, 105-124.
    • (1993) J. Molec. Biol. , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 152
    • 0025955186 scopus 로고
    • Atomic structure of the rapamycin human immunophilin FKBP-12 complex
    • Van Duyne, G. D., Standaert, R. F., Schreiber, S. L. and Clardy, J. (1991b) Atomic structure of the rapamycin human immunophilin FKBP-12 complex. J. Am. Chem. Soc. 113, 7433-7434.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 7433-7434
    • Van Duyne, G.D.1    Standaert, R.F.2    Schreiber, S.L.3    Clardy, J.4
  • 153
    • 0028674385 scopus 로고
    • Accounting for molecular mobility in structure determination based on nuclear magnetic resonance spectroscopic and X-ray diffraction data
    • van Gunsteren, W. F., Brunne, R. M., Gros, P., van Schaik, R. C., Schiffer, C. A. and Torda, A. E. (1994) Accounting for molecular mobility in structure determination based on nuclear magnetic resonance spectroscopic and X-ray diffraction data. Meths Enzymol. 239, 619-654.
    • (1994) Meths Enzymol. , vol.239 , pp. 619-654
    • Van Gunsteren, W.F.1    Brunne, R.M.2    Gros, P.3    Van Schaik, R.C.4    Schiffer, C.A.5    Torda, A.E.6
  • 154
    • 0030058373 scopus 로고    scopus 로고
    • A mean field model of ligand-protein interactions: Implications for the structural assessment of human immunodeficiency virus type 1 protease complexes and receptor-specific binding
    • Verkhivker, G. M. and Rejto, P. A. (1996) A mean field model of ligand-protein interactions: Implications for the structural assessment of human immunodeficiency virus type 1 protease complexes and receptor-specific binding. Proc. natn. Acad. Sci. U.S.A. 93, 60-64.
    • (1996) Proc. Natn. Acad. Sci. U.S.A. , vol.93 , pp. 60-64
    • Verkhivker, G.M.1    Rejto, P.A.2
  • 155
    • 0028773887 scopus 로고
    • Structure-based drug design: Progress, results and challenges
    • Verlinde, C. L. and Hol, W. G. (1994) Structure-based drug design: Progress, results and challenges. Structure 2, 577-587.
    • (1994) Structure , vol.2 , pp. 577-587
    • Verlinde, C.L.1    Hol, W.G.2
  • 156
    • 0029644728 scopus 로고
    • Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases
    • Vonrhein, C., Schlauderer, G. J. and Schulz, G. E. (1995) Movie of the structural changes during a catalytic cycle of nucleoside monophosphate kinases. Structure 3, 483-490.
    • (1995) Structure , vol.3 , pp. 483-490
    • Vonrhein, C.1    Schlauderer, G.J.2    Schulz, G.E.3
  • 157
    • 0028934005 scopus 로고
    • The importance of being floppy
    • Wagner, G. (1995) The importance of being floppy. Nature struct. Biol. 2, 255-257.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 255-257
    • Wagner, G.1
  • 158
    • 84988053694 scopus 로고
    • An all atom force field for simulations of proteins and nucleic acids
    • Weiner, S. J., Kollman, P. A., Nguyen, D. T. and Case, D. A. (1986) An all atom force field for simulations of proteins and nucleic acids. J. comput. Chem. 7, 230-252.
    • (1986) J. Comput. Chem. , vol.7 , pp. 230-252
    • Weiner, S.J.1    Kollman, P.A.2    Nguyen, D.T.3    Case, D.A.4
  • 159
    • 0027253014 scopus 로고
    • X-ray structures of two single-residue mutants of DNase I: H134Q and Y76A
    • Weston, S. and Suck, D. (1993) X-ray structures of two single-residue mutants of DNase I: H134Q and Y76A. Prot. Eng. 6, 349-357.
    • (1993) Prot. Eng. , vol.6 , pp. 349-357
    • Weston, S.1    Suck, D.2
  • 160
    • 0028233011 scopus 로고
    • Alternative native flap conformation revealed by 2.3 Å resolution structure of SIV proteinase
    • Wilderspin, A. F. and Sugrue, R. J. (1994) Alternative native flap conformation revealed by 2.3 Å resolution structure of SIV proteinase. J. molec. Biol. 239, 97-103.
    • (1994) J. Molec. Biol. , vol.239 , pp. 97-103
    • Wilderspin, A.F.1    Sugrue, R.J.2
  • 161
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson, I. A., Skehel, J. J. and Wiley, D. C. (1981) Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature 289, 366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 162
    • 0000838678 scopus 로고
    • Comparative X-ray structures of the major binding protein for the immunosuppressant FK506 (tacrolimus) in unliganded form and in complex with FK506 and rapamycin
    • Wilson, K. P., Yamashita, M. M., Sintchak, M. D., Rotstein, S. H., Murcko, M. A., Boger, J., Thomson, J. A., Fitzgibbon, M. J., Black, J. R. and Navia, M. A. (1995) Comparative X-ray structures of the major binding protein for the immunosuppressant FK506 (tacrolimus) in unliganded form and in complex with FK506 and rapamycin. Acta Cryst. D51, 511-521.
    • (1995) Acta Cryst. , vol.D51 , pp. 511-521
    • Wilson, K.P.1    Yamashita, M.M.2    Sintchak, M.D.3    Rotstein, S.H.4    Murcko, M.A.5    Boger, J.6    Thomson, J.A.7    Fitzgibbon, M.J.8    Black, J.R.9    Navia, M.A.10
  • 163
    • 0023120307 scopus 로고
    • Comparison of two highly refined structures of bovine pancreatic trypsin inhibitor
    • Wlodawer, A., Deisenhofer, J. and Huber, R. (1987) Comparison of two highly refined structures of bovine pancreatic trypsin inhibitor. J. molec. Biol. 193, 145-156.
    • (1987) J. Molec. Biol. , vol.193 , pp. 145-156
    • Wlodawer, A.1    Deisenhofer, J.2    Huber, R.3
  • 164
    • 0027218692 scopus 로고
    • Structure-based inhibitors of HIV-1 protease
    • Wlodawer, A. and Erickson, J. W. (1993) Structure-based inhibitors of HIV-1 protease. A. Rev. Biochem. 62, 543-585.
    • (1993) A. Rev. Biochem. , vol.62 , pp. 543-585
    • Wlodawer, A.1    Erickson, J.W.2
  • 165
    • 0024291642 scopus 로고
    • Structure of phosphate-free ribonuclease A refined at 1.26 Å
    • Wlodawer, A., Svensson, L. A., Sjolin, L. and Gilliland, G. L. (1988) Structure of phosphate-free ribonuclease A refined at 1.26 Å. Biochemistry 27, 2705-2717.
    • (1988) Biochemistry , vol.27 , pp. 2705-2717
    • Wlodawer, A.1    Svensson, L.A.2    Sjolin, L.3    Gilliland, G.L.4
  • 166
    • 0025194445 scopus 로고
    • 2.2 Å resolution structure analysis of two refined N-acetylneuraminyl-lactose-wheat germ agglutinin isolectin complexes
    • Wright, C. S. (1990) 2.2 Å resolution structure analysis of two refined N-acetylneuraminyl-lactose-wheat germ agglutinin isolectin complexes. J. molec. Biol. 215, 635-651.
    • (1990) J. Molec. Biol. , vol.215 , pp. 635-651
    • Wright, C.S.1
  • 167
    • 0028332168 scopus 로고
    • Correlated disorder of the pure Pro22/Leu25 form of crambin at 150 K refined to 1.05 Å resolution
    • Yamano, A. and Teeter, M. M. (1994) Correlated disorder of the pure Pro22/Leu25 form of crambin at 150 K refined to 1.05 Å resolution. J. biol. Chem. 269, 13,956-13,965.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13956-13965
    • Yamano, A.1    Teeter, M.M.2
  • 168
    • 0029986887 scopus 로고    scopus 로고
    • Crystal structures of CO-, deoxy-and met-myoglobins at various pH values
    • Yang, F. and Phillips, G. N. Jr. (1996) Crystal structures of CO-, deoxy-and met-myoglobins at various pH values. J. molec. Biol 256, 762-774.
    • (1996) J. Molec. Biol , vol.256 , pp. 762-774
    • Yang, F.1    Phillips G.N., Jr.2
  • 169
    • 0027468137 scopus 로고
    • Molecular dynamics simulation of HIV-1 protease in a crystalline environment and in solution
    • York, D. M., Darden, T. A., Pedersen, L. G. and Anderson, M. W. (1993) Molecular dynamics simulation of HIV-1 protease in a crystalline environment and in solution. Biochemistry 32, 1443-1453.
    • (1993) Biochemistry , vol.32 , pp. 1443-1453
    • York, D.M.1    Darden, T.A.2    Pedersen, L.G.3    Anderson, M.W.4
  • 170
    • 0027610433 scopus 로고
    • Comparison of radiation-induced decay and structure refinement from X-ray data collected from lysozyme crystals at low and ambient temperatures
    • Young, A. C. M., Dewan, J. C., Nave, C. and Tilton, R. F. (1993) Comparison of radiation-induced decay and structure refinement from X-ray data collected from lysozyme crystals at low and ambient temperatures. J. appl. Crystallogr. 26, 309-319.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 309-319
    • Young, A.C.M.1    Dewan, J.C.2    Nave, C.3    Tilton, R.F.4
  • 171
    • 0029644242 scopus 로고
    • Activity of the MAP kinase ERK2 is controlled by a flexible surface loop
    • Zhang, J., Zhang, F., Ebert, D., Cobb, M. H., Goldsmith, E. J. (1995a) Activity of the MAP kinase ERK2 is controlled by a flexible surface loop. Structure 3, 299-307.
    • (1995) Structure , vol.3 , pp. 299-307
    • Zhang, J.1    Zhang, F.2    Ebert, D.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 172
    • 0028001873 scopus 로고
    • Solid-state phase transition in the crystal structure of ribulose 1,5-bisphosphate carboxylase/oxygenase
    • Zhang, K. Y. J. and Eisenberg, D. (1994) Solid-state phase transition in the crystal structure of ribulose 1,5-bisphosphate carboxylase/oxygenase. Acta Cryst. D50, 258-262.
    • (1994) Acta Cryst. , vol.D50 , pp. 258-262
    • Zhang, K.Y.J.1    Eisenberg, D.2
  • 173
    • 0027093322 scopus 로고
    • Multiple alanine replacements within α-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability
    • Zhang, X. J., Baase, W. A. and Matthews, B. W. (1992) Multiple alanine replacements within α-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. Prot. Sci. 1, 761-776.
    • (1992) Prot. Sci. , vol.1 , pp. 761-776
    • Zhang, X.J.1    Baase, W.A.2    Matthews, B.W.3
  • 174
    • 0029150760 scopus 로고
    • Protein flexibility and adaptability seen in 25 crystal forms of T4 lyszyme
    • Zhang, X. J., Wozniak, J. A. and Matthews, B. W. (1995b) Protein flexibility and adaptability seen in 25 crystal forms of T4 lyszyme. J. molec. Biol. 250, 527-552.
    • (1995) J. Molec. Biol. , vol.250 , pp. 527-552
    • Zhang, X.J.1    Wozniak, J.A.2    Matthews, B.W.3


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