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Volumn 42, Issue 19, 2003, Pages 5837-5849

Hydrogen exchange kinetics of RNase A and the urea: TMAO paradigm

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN EXCHANGE KINETICS;

EID: 0038290339     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0206457     Document Type: Article
Times cited : (69)

References (70)
  • 2
    • 0020336190 scopus 로고
    • Living with water stress: Evolution of osmolyte systems
    • Yancey, P. H., Clark, M. E., Hand, S. C., Bowlus, R. D., and Somero, G. N. (1982) Living with water stress: evolution of osmolyte systems. Science 217, 1214-22.
    • (1982) Science , vol.217 , pp. 1214-1222
    • Yancey, P.H.1    Clark, M.E.2    Hand, S.C.3    Bowlus, R.D.4    Somero, G.N.5
  • 3
    • 0015406621 scopus 로고
    • Water Relations of Sugar-tolerant Yeasts: The Role of Intracellular Polyols
    • Brown, A. D., and Simpson, J. R. (1972) Water Relations of Sugar-tolerant Yeasts: the Role of Intracellular Polyols. J. Gen. Microbiol. 72, 589-591.
    • (1972) J. Gen. Microbiol. , vol.72 , pp. 589-591
    • Brown, A.D.1    Simpson, J.R.2
  • 4
    • 0015966621 scopus 로고
    • The salt relations of marine and halophilic species of the unicellular green alga. Dunaliella: The role of glycerol as a compatible solute
    • Borowitzka, L. J., and Brown, A. D. (1974) The salt relations of marine and halophilic species of the unicellular green alga. Dunaliella: The role of glycerol as a compatible solute. Arch. Microbiol. 96, 37-52.
    • (1974) Arch. Microbiol. , vol.96 , pp. 37-52
    • Borowitzka, L.J.1    Brown, A.D.2
  • 5
    • 0018474573 scopus 로고
    • Solute compatibility with enzyme function and structure: Rationales for the selection of osmotic agents and end-products of anaerobic metabolism in marine invertebrates
    • Bowlus, R. D., and Somero, G. N. (1979) Solute compatibility with enzyme function and structure: rationales for the selection of osmotic agents and end-products of anaerobic metabolism in marine invertebrates. J. Exp. Zool. 208, 137-51.
    • (1979) J. Exp. Zool. , vol.208 , pp. 137-151
    • Bowlus, R.D.1    Somero, G.N.2
  • 6
    • 0042404530 scopus 로고
    • Enzyme Activities in Concentrated Solutions of Glycinebetaine and Other Solutes
    • Pollard, A., and Wyn Jones, R. G. (1979) Enzyme Activities in Concentrated Solutions of Glycinebetaine and Other Solutes. Planta 144, 291-298.
    • (1979) Planta , vol.144 , pp. 291-298
    • Pollard, A.1    Wyn Jones, R.G.2
  • 7
    • 0029812281 scopus 로고    scopus 로고
    • Effect of proline on lactate dehydrogenase activity: Testing the generality and scope of the compatibility paradigm
    • Wang, A., and Bolen, D. W. (1996) Effect of proline on lactate dehydrogenase activity: Testing the generality and scope of the compatibility paradigm. Biophys. J. 71, 2117-2122.
    • (1996) Biophys. J. , vol.71 , pp. 2117-2122
    • Wang, A.1    Bolen, D.W.2
  • 8
    • 0018641198 scopus 로고
    • Counteraction of urea destabilization of protein structure by methylamine osmoregulatory compounds of elasmobranch fishes
    • Yancey, P. H., and Somero, G. N. (1979) Counteraction of urea destabilization of protein structure by methylamine osmoregulatory compounds of elasmobranch fishes. Biochem. J. 183, 317-323.
    • (1979) Biochem. J. , vol.183 , pp. 317-323
    • Yancey, P.H.1    Somero, G.N.2
  • 9
    • 0023030796 scopus 로고
    • Predominant osmotically active organic solutes in rat and rabbit renal medullas
    • Bagnasco, S., Balaban, R., Fales, H. M., Yang, Y. M., and Burg, M. (1986) Predominant osmotically active organic solutes in rat and rabbit renal medullas. J. Biol. Chem. 261, 5872-7.
    • (1986) J. Biol. Chem. , vol.261 , pp. 5872-5877
    • Bagnasco, S.1    Balaban, R.2    Fales, H.M.3    Yang, Y.M.4    Burg, M.5
  • 10
    • 0001784001 scopus 로고
    • Gilles, R., and Gilles-Baillien, M., Eds., Springer-Verlag, Berlin Heidelberg
    • Yancey, P. H. (1985) in Transport Processes, Iono- and Osmoregulation (Gilles, R., and Gilles-Baillien, M., Eds.) pp 424-436. Springer-Verlag, Berlin Heidelberg.
    • (1985) Transport Processes, Iono- and Osmoregulation , pp. 424-436
    • Yancey, P.H.1
  • 11
    • 0001315798 scopus 로고
    • Methylamine osmoregulatory solutes of elasmobranch fishes counteract urea inhibition of enzymes
    • Yancey, P. H., and Somero, G. N. (1980) Methylamine osmoregulatory solutes of elasmobranch fishes counteract urea inhibition of enzymes. J. Exp. Zool. 212, 205-213.
    • (1980) J. Exp. Zool. , vol.212 , pp. 205-213
    • Yancey, P.H.1    Somero, G.N.2
  • 12
    • 0025666432 scopus 로고
    • Importance of Organic Osmolytes for Osmoregulation by Renal Medullary Cells
    • Garcia-Perez, A., and Burg, M. B. (1990) Importance of Organic Osmolytes for Osmoregulation by Renal Medullary Cells. Hypertension 16, 595-602.
    • (1990) Hypertension , vol.16 , pp. 595-602
    • Garcia-Perez, A.1    Burg, M.B.2
  • 13
    • 0027483576 scopus 로고
    • Determinants of relative amounts of medullary organic osmolytes: Effects of NaCl and urea differ
    • Nakanishi, T., Uyama, O., Nakahama, H., Takamitsu, Y., and Sugita, M. (1993) Determinants of relative amounts of medullary organic osmolytes: effects of NaCl and urea differ. Am. J. Physiol. 264, F472-F479.
    • (1993) Am. J. Physiol. , vol.264
    • Nakanishi, T.1    Uyama, O.2    Nakahama, H.3    Takamitsu, Y.4    Sugita, M.5
  • 14
    • 0023777743 scopus 로고
    • Osmotic effectors in kidneys of xeric and mesic rodents: Corticomedullary distributions and changes with water availability
    • Yancey, P. H. (1988) Osmotic effectors in kidneys of xeric and mesic rodents: corticomedullary distributions and changes with water availability. J. Comp. Physiol. B 158, 369-380.
    • (1988) J. Comp. Physiol. B , vol.158 , pp. 369-380
    • Yancey, P.H.1
  • 15
    • 0001837325 scopus 로고
    • From dogfish to dogs: Trimethylamines protect proteins from urea
    • Somero, G. N. (1986) From dogfish to dogs: Trimethylamines protect proteins from urea. News Physiol. Sci. 1, 9-12.
    • (1986) News Physiol. Sci. , vol.1 , pp. 9-12
    • Somero, G.N.1
  • 16
    • 0029987341 scopus 로고    scopus 로고
    • Glycerophosphocholine and betaine counteract the effect of urea on pyruvate kinase
    • Burg, M. B., Kwon, E. D., and Peters, E. M. (1996) Glycerophosphocholine and betaine counteract the effect of urea on pyruvate kinase. Kidney Int. 50, S1-S5.
    • (1996) Kidney Int. , vol.50
    • Burg, M.B.1    Kwon, E.D.2    Peters, E.M.3
  • 17
    • 0031967834 scopus 로고    scopus 로고
    • Trimethylamine-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: A test of the counteraction hypothesis
    • Baskakov, I., Wang, A., and Bolen, D. W. (1998) Trimethylamine-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: a test of the counteraction hypothesis. Biophys. J. 74, 2666-73.
    • (1998) Biophys. J. , vol.74 , pp. 2666-2673
    • Baskakov, I.1    Wang, A.2    Bolen, D.W.3
  • 19
    • 0023444286 scopus 로고
    • Effects of urea and trimethylamine-N-oxide on enzyme activity and stability
    • Mashino, T., and Fridovich, I. (1987) Effects of urea and trimethylamine-N-oxide on enzyme activity and stability. Arch. Biochem. Biophys. 258, 356-360.
    • (1987) Arch. Biochem. Biophys. , vol.258 , pp. 356-360
    • Mashino, T.1    Fridovich, I.2
  • 20
    • 0031427001 scopus 로고    scopus 로고
    • Urea and methylamines have similar effects on aldose reductase activity
    • Burg, M. B., and Peters, E. M. (1997) Urea and methylamines have similar effects on aldose reductase activity. Am. J. Physiol. 276, F1048-53.
    • (1997) Am. J. Physiol. , vol.276
    • Burg, M.B.1    Peters, E.M.2
  • 23
    • 0035958656 scopus 로고    scopus 로고
    • The osmophobic effect: Natural selection of a thermodynamic force in protein folding
    • Bolen, D. W., and Baskakov, I. V. (2001) The osmophobic effect: natural selection of a thermodynamic force in protein folding. J. Mol. Biol. 310, 955-63.
    • (2001) J. Mol. Biol. , vol.310 , pp. 955-963
    • Bolen, D.W.1    Baskakov, I.V.2
  • 24
    • 0028960492 scopus 로고
    • How Valid Are Denaturant-induced Unfolding Free Energy Measurements? Level of Conformance to Common Assumptions over an Extended Range of Ribonuclease A Stability
    • Yao, M., and Bolen, D. W. (1995) How Valid Are Denaturant- induced Unfolding Free Energy Measurements? Level of Conformance to Common Assumptions over an Extended Range of Ribonuclease A Stability. Biochemistry 34, 3771-3779.
    • (1995) Biochemistry , vol.34 , pp. 3771-3779
    • Yao, M.1    Bolen, D.W.2
  • 25
    • 0000414455 scopus 로고
    • Hirs, C. H. W., and Timasheff, S. N., Eds., Academic Press, Inc
    • Pace, C. N. (1986) in Enzyme Structure, Part L (Hirs, C. H. W., and Timasheff, S. N., Eds.) pp 266-280, Academic Press, Inc.
    • (1986) Enzyme Structure, Part L , pp. 266-280
    • Pace, C.N.1
  • 26
    • 0030762556 scopus 로고    scopus 로고
    • A naturally occurring protective system in urea-rich cells: Mechanism of osmolyte protection of proteins against urea denaturation
    • Wang, A., and Bolen, D. W. (1997) A naturally occurring protective system in urea-rich cells: mechanism of osmolyte protection of proteins against urea denaturation. Biochemistry 36, 9101-8.
    • (1997) Biochemistry , vol.36 , pp. 9101-9108
    • Wang, A.1    Bolen, D.W.2
  • 29
    • 0028787409 scopus 로고
    • Effects of a naturally occurring compatible osmolyte on the internal dynamics of ribonuclease A
    • Wang, A., Robertson, A. D., and Bolen, D. W. (1995) Effects of a naturally occurring compatible osmolyte on the internal dynamics of ribonuclease A. Biochemistry 34, 15096-15104.
    • (1995) Biochemistry , vol.34 , pp. 15096-15104
    • Wang, A.1    Robertson, A.D.2    Bolen, D.W.3
  • 30
    • 0024473985 scopus 로고
    • Sequential H NMR assignment and solution structure of bovine pancreatic ribonuclease A
    • Rico, M., Santoro, J., Gonzalez, C., Neira, J. L., Nieto, J. L., and Herranz, J. (1989) Sequential H NMR assignment and solution structure of bovine pancreatic ribonuclease A. Eur. J. Biochem. 183, 623-638.
    • (1989) Eur. J. Biochem. , vol.183 , pp. 623-638
    • Rico, M.1    Santoro, J.2    Gonzalez, C.3    Neira, J.L.4    Nieto, J.L.5    Herranz, J.6
  • 31
    • 0024384662 scopus 로고
    • Proton NMR Assignments and Regular Backbone Structure of Bovine Pancreatic Ribonuclease A in Aqueous Solution
    • Robertson, A. D., Purisima, E. O., Eastman, M. A., and Scheraga, H. A. (1989) Proton NMR Assignments and Regular Backbone Structure of Bovine Pancreatic Ribonuclease A in Aqueous Solution. Biochemistry 28, 5930-5938.
    • (1989) Biochemistry , vol.28 , pp. 5930-5938
    • Robertson, A.D.1    Purisima, E.O.2    Eastman, M.A.3    Scheraga, H.A.4
  • 32
    • 0024977344 scopus 로고
    • NMR studies of the influence of dodecyl sulfate on the amide hydrogen exchange kinetics of a micelle-solubilized hydrophobic tripeptide
    • O'Neil, J. D. J., and Sykes, B. D. (1989) NMR studies of the influence of dodecyl sulfate on the amide hydrogen exchange kinetics of a micelle-solubilized hydrophobic tripeptide. Biochemistry 28, 699-707.
    • (1989) Biochemistry , vol.28 , pp. 699-707
    • O'Neil, J.D.J.1    Sykes, B.D.2
  • 33
    • 33846851242 scopus 로고
    • Study of moderately rapid chemical exchange reactions by means of nuclear magnetic double resonance
    • Forsen, S., and Hoffman, R. A. (1963) Study of moderately rapid chemical exchange reactions by means of nuclear magnetic double resonance. J. Chem. Phys. 39, 2892-2901.
    • (1963) J. Chem. Phys. , vol.39 , pp. 2892-2901
    • Forsen, S.1    Hoffman, R.A.2
  • 34
    • 0022745510 scopus 로고
    • pH dependence of HX from backbone peptide amides in Apamin
    • Dempsey, C. E. (1986) pH dependence of HX from backbone peptide amides in Apamin. Biochemistry 25, 3904-3911.
    • (1986) Biochemistry , vol.25 , pp. 3904-3911
    • Dempsey, C.E.1
  • 35
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro, M. M., and Bolen, D. W. (1988) Unfolding Free Energy Changes Determined by the Linear Extrapolation Method. 1. Unfolding of Phenylmethanesulfonyl α-Chymotrypsin Using Different Denaturants. Biochemistry 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 37
    • 0023056528 scopus 로고
    • Effects of denaturants on amide proton exchange rates: A test for structure in protein fragments and folding intermediates
    • Loftus, D., Gbenle, G. O., Kim, P. S., and Baldwin, R. L. (1986) Effects of denaturants on amide proton exchange rates: a test for structure in protein fragments and folding intermediates. Biochemistry 25, 1428-36.
    • (1986) Biochemistry , vol.25 , pp. 1428-1436
    • Loftus, D.1    Gbenle, G.O.2    Kim, P.S.3    Baldwin, R.L.4
  • 38
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • Hvidt, A., and 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
  • 40
    • 0027504749 scopus 로고
    • Hydrogen exchange identifies native-state motional domains important in protein folding
    • Kim, K.-S., Fuchs, J. A., and Woodward, C. K. (1993) Hydrogen Exchange Identifies Native-State Motional domains Important in Protein Folding. Biochemistry 32, 9600-9608.
    • (1993) Biochemistry , vol.32 , pp. 9600-9608
    • Kim, K.-S.1    Fuchs, J.A.2    Woodward, C.K.3
  • 41
    • 0030334648 scopus 로고    scopus 로고
    • An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway
    • Clarke, J., and Fersht, A. R. (1996) An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway. Folding Des. 1, 243-254.
    • (1996) Folding Des. , vol.1 , pp. 243-254
    • Clarke, J.1    Fersht, A.R.2
  • 42
    • 0030047378 scopus 로고    scopus 로고
    • Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain
    • Swint-Kruse, L., and Robertson, A. D. (1996) Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain. Biochemistry 35, 171-80.
    • (1996) Biochemistry , vol.35 , pp. 171-180
    • Swint-Kruse, L.1    Robertson, A.D.2
  • 43
    • 0032539953 scopus 로고    scopus 로고
    • Local dynamics and stability of apocytochrome b562 examined by hydrogen exchange
    • Fuentes, E. J., and Wand, A. J. (1998) Local dynamics and stability of apocytochrome b562 examined by hydrogen exchange. Biochemistry 37, 3687-98.
    • (1998) Biochemistry , vol.37 , pp. 3687-3698
    • Fuentes, E.J.1    Wand, A.J.2
  • 44
    • 0030840017 scopus 로고    scopus 로고
    • Microsecond protein folding kinetics from native-state hydrogen exchange
    • Arrington, C. B., and Robertson, A. D. (1997) Microsecond protein folding kinetics from native-state hydrogen exchange. Biochemistry 36, 8686-91.
    • (1997) Biochemistry , vol.36 , pp. 8686-8691
    • Arrington, C.B.1    Robertson, A.D.2
  • 45
    • 0035075187 scopus 로고    scopus 로고
    • Kinetics of unfolding and folding from amide hydrogen exchange in native ubiquitin
    • Sivaraman, T., Arrington, C. B., and Robertson, A. D. (2001) Kinetics of unfolding and folding from amide hydrogen exchange in native ubiquitin. Nat. Struct. Biol. 8, 331-3.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 331-333
    • Sivaraman, T.1    Arrington, C.B.2    Robertson, A.D.3
  • 46
    • 0026446531 scopus 로고
    • Nuclear magnetic resonance studies of the internal dynamics in Apo, (Cd2+)1 and (Ca2+)2 calbindin D9k. The rates of amide proton exchange with solvent
    • Skelton, N. J., Kordel, J., Akke, M., and Chazin, W. J. (1992) Nuclear magnetic resonance studies of the internal dynamics in Apo, (Cd2+)1 and (Ca2+)2 calbindin D9k. The rates of amide proton exchange with solvent. J. Mol. Biol. 227, 1100-17.
    • (1992) J. Mol. Biol. , vol.227 , pp. 1100-1117
    • Skelton, N.J.1    Kordel, J.2    Akke, M.3    Chazin, W.J.4
  • 48
    • 0027730340 scopus 로고
    • Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A
    • Mayo, S. L., and Baldwin, R. L. (1993) Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A. Science 262, 873-876.
    • (1993) Science , vol.262 , pp. 873-876
    • Mayo, S.L.1    Baldwin, R.L.2
  • 49
    • 0033555835 scopus 로고    scopus 로고
    • Hydrogen exchange in ribonuclease A and ribonuclease S: Evidence for residual structure in the unfolded state under native conditions
    • Neira, J. L., Sevilla, P., Menendez, M., Bruix, M., and Rico, M. (1999) Hydrogen exchange in ribonuclease A and ribonuclease S: evidence for residual structure in the unfolded state under native conditions. J. Mol. Biol. 285, 627-43.
    • (1999) J. Mol. Biol. , vol.285 , pp. 627-643
    • Neira, J.L.1    Sevilla, P.2    Menendez, M.3    Bruix, M.4    Rico, M.5
  • 50
    • 0019076960 scopus 로고
    • Hydrogen isotope exchange kinetics of single protons in Bovine pancreatic trypsin inhibitor
    • Woodward, C., and Hilton, B. (1980) Hydrogen isotope exchange kinetics of single protons in Bovine pancreatic trypsin inhibitor. Biophys. J. 32, 561-576.
    • (1980) Biophys. J. , vol.32 , pp. 561-576
    • Woodward, C.1    Hilton, B.2
  • 51
    • 0020493395 scopus 로고
    • Hydrogen exchange rates and the dynamic structure of proteins
    • Woodward, C., Simon, I., and Tuchsen, E. (1982) Hydrogen exchange rates and the dynamic structure of proteins. Mol. Cell Biochem. 48, 135-160.
    • (1982) Mol. Cell Biochem. , vol.48 , pp. 135-160
    • Woodward, C.1    Simon, I.2    Tuchsen, E.3
  • 52
    • 0027977883 scopus 로고
    • Protein hydrogen exchange in denaturant: Quantitative analysis by a two-process model
    • Qian, H., Mayo, S. L., and Morton, A. (1994) Protein Hydrogen Exchange in Denaturant: Quantitative Analysis by a Two-Process Model. Biochemistry 33, 8167-8171.
    • (1994) Biochemistry , vol.33 , pp. 8167-8171
    • Qian, H.1    Mayo, S.L.2    Morton, A.3
  • 53
    • 0029872925 scopus 로고    scopus 로고
    • A general two-process model describes the hydrogen exchange behavior of RNase A in unfolding conditions
    • Loh, S. N., Rohl, C. A., Kiefhaber, T., and Baldwin, R. L. (1996) A general two-process model describes the hydrogen exchange behavior of RNase A in unfolding conditions. Proc. Natl. Acad. Sci. U.S.A. 93, 1982-7.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1982-1987
    • Loh, S.N.1    Rohl, C.A.2    Kiefhaber, T.3    Baldwin, R.L.4
  • 54
    • 0028862864 scopus 로고
    • The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes
    • Liu, Y., and Bolen, D. W. (1995) The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes. Biochemistry 34, 12884-12891.
    • (1995) Biochemistry , vol.34 , pp. 12884-12891
    • Liu, Y.1    Bolen, D.W.2
  • 55
    • 0001244253 scopus 로고
    • Urea-requiring lactate dehydrogenases of marine elasmobranch fishes
    • Yancey, P. H., and Somero, G. N. (1978) Urea-Requiring Lactate Dehydrogenases of Marine Elasmobranch Fishes. J. Comp. Physiol. 125, 135-141.
    • (1978) J. Comp. Physiol. , vol.125 , pp. 135-141
    • Yancey, P.H.1    Somero, G.N.2
  • 56
    • 0034003742 scopus 로고    scopus 로고
    • Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide
    • Jaravine, V. A., Rathgeb-Szabo, K., and Alexandrescu, A. T. (2000) Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N- oxide. Protein Sci. 9, 290-301.
    • (2000) Protein Sci. , vol.9 , pp. 290-301
    • Jaravine, V.A.1    Rathgeb-Szabo, K.2    Alexandrescu, A.T.3
  • 57
    • 0033593247 scopus 로고    scopus 로고
    • Defining protein ensembles with native-state NH exchange: Kinetics of interconversion and cooperative units from combined NMR and MS analysis
    • Arrington, C. B., Teesch, L. M., and Robertson, A. D. (1999) Defining protein ensembles with native-state NH exchange: kinetics of interconversion and cooperative units from combined NMR and MS analysis. J. Mol. Biol, 285, 1265-75.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1265-1275
    • Arrington, C.B.1    Teesch, L.M.2    Robertson, A.D.3
  • 58
    • 0034733386 scopus 로고    scopus 로고
    • Correlated motions in native proteins from MS analysis of NH exchange: Evidence for a manifold of unfolding reactions in ovomucoid third domain
    • Arrington, C. B., and Robertson, A. D. (2000) Correlated motions in native proteins from MS analysis of NH exchange: evidence for a manifold of unfolding reactions in ovomucoid third domain. J. Mol. Biol. 300, 221-32.
    • (2000) J. Mol. Biol. , vol.300 , pp. 221-232
    • Arrington, C.B.1    Robertson, A.D.2
  • 59
    • 0030334648 scopus 로고    scopus 로고
    • An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway
    • Clarke, J., and Fersht, A. R. (1996) An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway. Fold Des. 1, 243-54.
    • (1996) Fold Des. , vol.1 , pp. 243-254
    • Clarke, J.1    Fersht, A.R.2
  • 60
    • 0032570873 scopus 로고    scopus 로고
    • Forcing thermodynamically unfolded proteins to fold
    • Baskakov, I., and Bolen, D. W. (1998) Forcing thermodynamically unfolded proteins to fold. J. Biol. Chem. 273, 4831-4.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4831-4834
    • Baskakov, I.1    Bolen, D.W.2
  • 61
    • 0032483027 scopus 로고    scopus 로고
    • Osmolyte-driven contraction of a random coil protein
    • Qu, Y., Bolen, C. L., and Bolen, D. W. (1998) Osmolyte-driven contraction of a random coil protein. Proc. Natl. Acad. Sci. U.S.A. 95, 9268-73.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 9268-9273
    • Qu, Y.1    Bolen, C.L.2    Bolen, D.W.3
  • 63
    • 0031908874 scopus 로고    scopus 로고
    • Hydrogen exchange studies of protein structure
    • Raschke, T. M., and Marqusee, S. (1998) Hydrogen exchange studies of protein structure. Curr. Opin. Biotechnol. 9, 80-6.
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 80-86
    • Raschke, T.M.1    Marqusee, S.2
  • 64
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai, Y., Sosnick, T. R., Mayne, L., and Englander, S. W. (1995) Protein folding intermediates: Native-state hydrogen exchange. Science 269, 192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 65
    • 0037108164 scopus 로고    scopus 로고
    • Populating partially unfolded forms by hydrogen exchange-directed protein engineering
    • Takei, J., Pei, W., Vu, D., and Bai, Y. (2002) Populating partially unfolded forms by hydrogen exchange-directed protein engineering. Biochemistry 41, 12308-12.
    • (2002) Biochemistry , vol.41 , pp. 12308-12312
    • Takei, J.1    Pei, W.2    Vu, D.3    Bai, Y.4
  • 66
    • 0034636991 scopus 로고    scopus 로고
    • Ensemble modulation as an origin of denaturant-independent hydrogen exchange in proteins
    • Wooll, J. O., Wrabl, J. O., and Hilser, V. J. (2000) Ensemble modulation as an origin of denaturant-independent hydrogen exchange in proteins. J. Mol. Biol. 301, 247-56.
    • (2000) J. Mol. Biol. , vol.301 , pp. 247-256
    • Wooll, J.O.1    Wrabl, J.O.2    Hilser, V.J.3
  • 67
    • 0034622669 scopus 로고    scopus 로고
    • 31P and 1H NMR studies of the effect of the counteracting osmolyte trimethylamine-N-oxide on interactions of urea with ribonuclease A
    • Palmer, H. R., Bedford, J. J., Leader, J. P., and Smith, R. A. (2000) 31P and 1H NMR studies of the effect of the counteracting osmolyte trimethylamine-N-oxide on interactions of urea with ribonuclease A. J. Biol. Chem. 275, 27708-11.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27708-27711
    • Palmer, H.R.1    Bedford, J.J.2    Leader, J.P.3    Smith, R.A.4
  • 68
    • 0034642225 scopus 로고    scopus 로고
    • Effects of guanidine hydrochloride on the proton inventory of proteins: Implications on interpretations of protein stability
    • Bolen, D. W., and Yang, M. (2000) Effects of guanidine hydrochloride on the proton inventory of proteins: implications on interpretations of protein stability. Biochemistry 39, 15208-16.
    • (2000) Biochemistry , vol.39 , pp. 15208-15216
    • Bolen, D.W.1    Yang, M.2
  • 69
    • 0035977663 scopus 로고    scopus 로고
    • No effect of trimethylamine N-oxide on the internal dynamics of the protein native fold
    • Gonnelli, M., and Strambini, G. B. (2001) No effect of trimethylamine N-oxide on the internal dynamics of the protein native fold. Biophys. Chem. 89, 77-85.
    • (2001) Biophys. Chem. , vol.89 , pp. 77-85
    • Gonnelli, M.1    Strambini, G.B.2
  • 70
    • 0037076522 scopus 로고    scopus 로고
    • Evidence for flexibility in the function of ribonuclease A
    • Cole, R., and Loria, J. P. (2002) Evidence for flexibility in the function of ribonuclease A. Biochemistry 41, 6072-81.
    • (2002) Biochemistry , vol.41 , pp. 6072-6081
    • Cole, R.1    Loria, J.P.2


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