메뉴 건너뛰기




Volumn 276, Issue 3, 1998, Pages 647-656

Folding intermediates of wild-type and mutants of barnase. II. Correlation of changes in equilibrium amide exchange kinetics with the population of the folding intermediate

Author keywords

Barnase; Hydrogen exchange; Protein folding; Stability

Indexed keywords

BARNASE; MUTANT PROTEIN; RIBONUCLEASE; UNCLASSIFIED DRUG;

EID: 0032570757     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1547     Document Type: Article
Times cited : (29)

References (32)
  • 1
    • 0028806684 scopus 로고
    • A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: Implications for the initiation of protein folding
    • Arcus V. L., Vuilleumier S., Freund S. M. V., Bycroft M., Fersht A. R. A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding. J. Mol. Biol. 254:1995;305-321.
    • (1995) J. Mol. Biol. , vol.254 , pp. 305-321
    • Arcus, V.L.1    Vuilleumier, S.2    Freund, S.M.V.3    Bycroft, M.4    Fersht, A.R.5
  • 3
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai Y., Sosnick T. R., Mayne L., Englander S. W. Protein folding intermediates: native-state hydrogen exchange. Science. 269:1995;192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 4
    • 0029746061 scopus 로고    scopus 로고
    • Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH
    • Chamberlain A. K., Handel T. M., Marqusee S. Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. Nature Struct. Biol. 3:1996;782-787.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 782-787
    • Chamberlain, A.K.1    Handel, T.M.2    Marqusee, S.3
  • 5
    • 0027155577 scopus 로고
    • Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation
    • Clarke J., Fersht A. R. Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation. Biochemistry. 32:1993;4322-4329.
    • (1993) Biochemistry , vol.32 , pp. 4322-4329
    • Clarke, J.1    Fersht, A.R.2
  • 6
    • 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., Fersht A. R. An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway. Folding & Design. 1:1996;243-254.
    • (1996) Folding & Design , vol.1 , pp. 243-254
    • Clarke, J.1    Fersht, A.R.2
  • 7
    • 0027505050 scopus 로고
    • Local breathing and global unfolding in hydrogen-exchange of barnase and its relationship to protein folding pathways
    • Clarke J., Hounslow A. M., Bycroft M., Fersht A. R. Local breathing and global unfolding in hydrogen-exchange of barnase and its relationship to protein folding pathways. Proc. Natl Acad. Sci. USA. 90:1993;9837-9841.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9837-9841
    • Clarke, J.1    Hounslow, A.M.2    Bycroft, M.3    Fersht, A.R.4
  • 8
    • 0032570532 scopus 로고    scopus 로고
    • Folding intermediates of wild-type and mutants of barnase. I. Use of φ-value analysis and m -values to probe the cooperative nature of the folding pre-equilibrium
    • Dalby P. A., Oliveberg M., Fersht A. R. Folding intermediates of wild-type and mutants of barnase. I. Use of φ-value analysis and m -values to probe the cooperative nature of the folding pre-equilibrium. J. Mol. Biol. 276:1998;625-646.
    • (1998) J. Mol. Biol. , vol.276 , pp. 625-646
    • Dalby, P.A.1    Oliveberg, M.2    Fersht, A.R.3
  • 9
    • 0023645482 scopus 로고
    • Electrostatic effects and hydrogen exchange behaviour in proteins: The pH dependence of exchange rates in lysozyme
    • Delepierre M., Dobson C. M., Karplus M., Poulsen F. M., States D. J., Wedin R. E. Electrostatic effects and hydrogen exchange behaviour in proteins: the pH dependence of exchange rates in lysozyme. J. Mol. Biol. 197:1987;111-130.
    • (1987) J. Mol. Biol. , vol.197 , pp. 111-130
    • Delepierre, M.1    Dobson, C.M.2    Karplus, M.3    Poulsen, F.M.4    States, D.J.5    Wedin, R.E.6
  • 10
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • Englander S. W., Kallenbach N. R. Hydrogen exchange and structural dynamics of proteins and nucleic acids. Quart. Rev. Biophys. 16:1984;521-655.
    • (1984) Quart. Rev. Biophys. , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 12
    • 6444222991 scopus 로고
    • Use of a glass electrode to measure acidities in deuterium oxide
    • Glasoe P. F., Long F. A. Use of a glass electrode to measure acidities in deuterium oxide. J. Phys. Chem. 64:1960;188-193.
    • (1960) J. Phys. Chem. , vol.64 , pp. 188-193
    • Glasoe, P.F.1    Long, F.A.2
  • 14
    • 0025337398 scopus 로고
    • Role of arginine 67 in the stabilization of chymotrypsin inhibitor 2: Examination of amide proton exchange rates and denaturation thermodynamics of an engineered protein
    • Jandu S. K., Ray S., Brooks L., Leatherbarrow R. J. Role of arginine 67 in the stabilization of chymotrypsin inhibitor 2: examination of amide proton exchange rates and denaturation thermodynamics of an engineered protein. Biochemistry. 29:1990;6264-6269.
    • (1990) Biochemistry , vol.29 , pp. 6264-6269
    • Jandu, S.K.1    Ray, S.2    Brooks, L.3    Leatherbarrow, R.J.4
  • 15
    • 0029061516 scopus 로고
    • Protein stability as a function of denaturant concentration: The thermal stability of barnase in the presence of urea
    • Johnson C. M., Fersht A. R. Protein stability as a function of denaturant concentration: the thermal stability of barnase in the presence of urea. Biochemistry. 34:1995;6795-6804.
    • (1995) Biochemistry , vol.34 , pp. 6795-6804
    • Johnson, C.M.1    Fersht, A.R.2
  • 16
    • 0027375522 scopus 로고
    • Protein internal flexibility and global stability: Effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor
    • Kim K.-S., Woodward C. Protein internal flexibility and global stability: effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor. Biochemistry. 32:1993;9609-9613.
    • (1993) Biochemistry , vol.32 , pp. 9609-9613
    • Kim, K.-S.1    Woodward, C.2
  • 18
    • 0029872925 scopus 로고    scopus 로고
    • A general two-process model describes the hydrogen exchange behaviour of RNase A in unfolding conditions
    • Loh S. N., Rohl C. A., Kiefhaber T., Baldwin R. L. A general two-process model describes the hydrogen exchange behaviour of RNase A in unfolding conditions. Proc. Natl Acad. Sci. USA. 93:1996;1982-1987.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 1982-1987
    • Loh, S.N.1    Rohl, C.A.2    Kiefhaber, T.3    Baldwin, R.L.4
  • 19
    • 0025698613 scopus 로고
    • Transient folding intermediates characterized by protein engineering
    • Matouschek A., Kellis J. Jr, Serrano L., Bycroft M., Fersht A. R. Transient folding intermediates characterized by protein engineering. Nature. 346:1990;440-445.
    • (1990) Nature , vol.346 , pp. 440-445
    • Matouschek, A.1    Kellis J., Jr.2    Serrano, L.3    Bycroft, M.4    Fersht, A.R.5
  • 20
    • 0028168139 scopus 로고
    • Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions
    • Matouschek A., Matthews J. M., Johnson C. M., Fersht A. R. Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions. Protein Eng. 7:1994;1089-1095.
    • (1994) Protein Eng. , vol.7 , pp. 1089-1095
    • Matouschek, A.1    Matthews, J.M.2    Johnson, C.M.3    Fersht, A.R.4
  • 21
    • 0026550397 scopus 로고
    • The folding of an enzyme IV. Structure of an intermediate in the refolding of barnase anaylsed by a protein engineering procedure
    • Matouschek A., Serrano L., Fersht A. R. The folding of an enzyme IV. Structure of an intermediate in the refolding of barnase anaylsed by a protein engineering procedure. J. Mol. Biol. 224:1992;819-835.
    • (1992) J. Mol. Biol. , vol.224 , pp. 819-835
    • Matouschek, A.1    Serrano, L.2    Fersht, A.R.3
  • 22
    • 0031552596 scopus 로고    scopus 로고
    • Hydrogen exchange in chymotrypsin inhibitor 2: Probed by mutagenesis
    • Neira J. L., Itzhaki L. S., Otzen D. E., Davis B., Fersht A. R. Hydrogen exchange in chymotrypsin inhibitor 2: probed by mutagenesis. J. Mol. Biol. 270:1997;99-110.
    • (1997) J. Mol. Biol. , vol.270 , pp. 99-110
    • Neira, J.L.1    Itzhaki, L.S.2    Otzen, D.E.3    Davis, B.4    Fersht, A.R.5
  • 23
    • 0029988634 scopus 로고    scopus 로고
    • Thermodynamics of transient conformations in the protein folding pathway of barnase: Reorganization of the folding intermediate at low pH
    • Oliveberg M., Fersht A. R. Thermodynamics of transient conformations in the protein folding pathway of barnase: reorganization of the folding intermediate at low pH. Biochemistry. 35:1996;2738-2749.
    • (1996) Biochemistry , vol.35 , pp. 2738-2749
    • Oliveberg, M.1    Fersht, A.R.2
  • 26
    • 0029153539 scopus 로고
    • Relationship between equilibrium amide proton exchange behaviour and the folding pathway of barnase
    • Perrett S., Clarke J., Hounslow A. M., Fersht A. R. Relationship between equilibrium amide proton exchange behaviour and the folding pathway of barnase. Biochemistry. 34:1995;9288-9298.
    • (1995) Biochemistry , vol.34 , pp. 9288-9298
    • Perrett, S.1    Clarke, J.2    Hounslow, A.M.3    Fersht, A.R.4
  • 28
    • 0024972479 scopus 로고
    • Capping and α-helix stability
    • Serrano L., Fersht A. R. Capping and α-helix stability. Nature. 342:1989;296-299.
    • (1989) Nature , vol.342 , pp. 296-299
    • Serrano, L.1    Fersht, A.R.2
  • 29
    • 0026579572 scopus 로고
    • The folding of an enzyme III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure
    • Serrano L., Matouschek A., Fersht A. R. The folding of an enzyme III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure. J. Mol. Biol. 224:1992;805-818.
    • (1992) J. Mol. Biol. , vol.224 , pp. 805-818
    • Serrano, L.1    Matouschek, A.2    Fersht, A.R.3
  • 31
    • 0030047378 scopus 로고    scopus 로고
    • Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain
    • Swint-Kruse L., Robertson A. D. Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain. Biochemistry. 35:1996;171-180.
    • (1996) Biochemistry , vol.35 , pp. 171-180
    • Swint-Kruse, L.1    Robertson, A.D.2
  • 32
    • 0020711969 scopus 로고
    • Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes
    • Wagner G. Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes. Quart. Rev. Biophys. 16:1983;1-57.
    • (1983) Quart. Rev. Biophys. , vol.16 , pp. 1-57
    • Wagner, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.