메뉴 건너뛰기




Volumn 41, Issue 40, 2002, Pages 12093-12099

The influence of intramolecular bridges on the dynamics of a protein folding reaction

Author keywords

[No Author keywords available]

Indexed keywords

INTRAMOLECULAR BRIDGES;

EID: 0037044333     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi026398o     Document Type: Article
Times cited : (23)

References (32)
  • 1
    • 0024358426 scopus 로고
    • Mapping the transition-state and pathway of protein folding by protein engineering
    • Matouschek, A., Kellis, I. T., Serrano, I., and Fersht, A. R. (1989) Mapping the transition-state and pathway of protein folding by protein engineering. Nature 340, 122-126.
    • (1989) Nature , vol.340 , pp. 122-126
    • Matouschek, A.1    Kellis, I.T.2    Serrano, I.3    Fersht, A.R.4
  • 2
    • 0031043161 scopus 로고    scopus 로고
    • Nucleation mechanisms in protein folding
    • Fersht, A. R. (1997) Nucleation mechanisms in protein folding. Curr. Opin. Struct. Biol. 7, 3-9.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 3-9
    • Fersht, A.R.1
  • 3
    • 0032411029 scopus 로고    scopus 로고
    • Sequence does specify protein conformation
    • Ellis, R. J., Dobson, C., and Hartl, U. (1998) Sequence does specify protein conformation. Trends Biochem. Sci. 23, 468-468.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 468
    • Ellis, R.J.1    Dobson, C.2    Hartl, U.3
  • 4
    • 0026653655 scopus 로고
    • Protein folding studied using hydrogen-exchange labeling and 2-dimensional NMR
    • Englander, S. W., and Mayne, L. (1993) Protein folding studied using hydrogen-exchange labeling and 2-dimensional NMR. Annu. Rev. Biophys. Biomol. Struct. 21, 243-265.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 243-265
    • Englander, S.W.1    Mayne, L.2
  • 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., and Fersht, A. R. (1993) Engineered disulfide bonds as probes of the folding pathway of barnase-increasing the stability of proteins against the rate of denaturation. Biochemistry 32, 4322-4329.
    • (1993) Biochemistry , vol.32 , pp. 4322-4329
    • Clarke, J.1    Fersht, A.R.2
  • 6
    • 0034602924 scopus 로고    scopus 로고
    • The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: The role of each disulfide bridge
    • Yokota and Segawa, S. (2000) The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridge. J. Mol. Biol. 295, 1275-1288.
    • (2000) J. Mol. Biol. , vol.295 , pp. 1275-1288
    • Yokota1    Segawa, S.2
  • 7
    • 0034697986 scopus 로고    scopus 로고
    • What can disulfide bonds tell us about protein energetics, function and folding: Simulations and bioinformatics analysis
    • Abkevich, V. I., and Shakhnovich, E. I. (2000) What can disulfide bonds tell us about protein energetics, function and folding: simulations and bioinformatics analysis. J. Mol. Biol. 300, 975-985.
    • (2000) J. Mol. Biol. , vol.300 , pp. 975-985
    • Abkevich, V.I.1    Shakhnovich, E.I.2
  • 9
    • 0031892524 scopus 로고    scopus 로고
    • Topology, sequence evolution and folding dynamics of an immunoglobulin domain
    • Parker, M. J., Dempsey, C. E., Hosszu, L. P., Waltho, J. P., and Clarke, A. R. (1998) Topology, sequence evolution and folding dynamics of an immunoglobulin domain. Nat. Struct. Biol. 5, 194-198.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 194-198
    • Parker, M.J.1    Dempsey, C.E.2    Hosszu, L.P.3    Waltho, J.P.4    Clarke, A.R.5
  • 10
    • 0032562178 scopus 로고    scopus 로고
    • Thermodynamic properties of transient intermediates and transition states in the folding of two contrasting protein structures
    • Parker, M. J., Lorch, M., Sessions, R. B., and Clarke (1998) Thermodynamic properties of transient intermediates and transition states in the folding of two contrasting protein structures. Biochemistry 37, 2538-2545.
    • (1998) Biochemistry , vol.37 , pp. 2538-2545
    • Parker, M.J.1    Lorch, M.2    Sessions, R.B.3    Clarke4
  • 11
    • 0033604845 scopus 로고    scopus 로고
    • Effects of core mutations on the folding of a beta-sheet protein: Implications for backbone organization in the I-state
    • Lorch, M., Mason, J. M., Clarke, A. R., and Parker, M. J. (1999) Effects of core mutations on the folding of a beta-sheet protein: implications for backbone organization in the I-state. Biochemistry 38, 1377-1385.
    • (1999) Biochemistry , vol.38 , pp. 1377-1385
    • Lorch, M.1    Mason, J.M.2    Clarke, A.R.3    Parker, M.J.4
  • 12
    • 0030871209 scopus 로고    scopus 로고
    • Acquisition of native beta-strand topology during the rapid collapse phase of protein folding
    • Parker, M. J., Dempsey, C. E., Lorch, M., and Clarke, A. R. (1997) Acquisition of native beta-strand topology during the rapid collapse phase of protein folding. Biochemistry 36, 13396-13405.
    • (1997) Biochemistry , vol.36 , pp. 13396-13405
    • Parker, M.J.1    Dempsey, C.E.2    Lorch, M.3    Clarke, A.R.4
  • 13
    • 0031735020 scopus 로고    scopus 로고
    • Determinants of strand register in antiparallel beta-sheets of proteins
    • Hutchinson, E. G., Sessions, R. B., Thornton, J. M., and Woolfson (1998) Determinants of strand register in antiparallel beta-sheets of proteins. Protein Sci. 7, 2287-2300.
    • (1998) Protein Sci. , vol.7 , pp. 2287-2300
    • Hutchinson, E.G.1    Sessions, R.B.2    Thornton, J.M.3    Woolfson4
  • 14
    • 0029058159 scopus 로고
    • An analysis of side-chain interactions and pair correlations within antiparallel beta-sheets-the differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs
    • Wouters, M. A., and Curmi, P. M. G. (1995) An analysis of side-chain interactions and pair correlations within antiparallel beta-sheets-the differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs. Proteins: Struct., Funct., Genet. 22, 119-131.
    • (1995) Proteins: Struct., Funct., Genet. , vol.22 , pp. 119-131
    • Wouters, M.A.1    Curmi, P.M.G.2
  • 15
    • 0024972502 scopus 로고
    • Substantial increase of protein stability by multiple disulfide bonds
    • Matsumura, M., Signor, G., and Matthews, B. (1989) Substantial increase of protein stability by multiple disulfide bonds. Nature 342, 291-293.
    • (1989) Nature , vol.342 , pp. 291-293
    • Matsumura, M.1    Signor, G.2    Matthews, B.3
  • 16
    • 0041089466 scopus 로고    scopus 로고
    • Effect of preformed correct tertiary interactions on rapid two state Tendamistat folding: Evidence for hairpins as initiation sites for β-sheet formation
    • Schonbrunner, N., Pappenburger, G., Scharf, M., Engels, J., and Kiefhaber, T. (1997) Effect of preformed correct tertiary interactions on rapid two state Tendamistat folding: evidence for hairpins as initiation sites for β-sheet formation. Biochemistry 36, 9057-9065.
    • (1997) Biochemistry , vol.36 , pp. 9057-9065
    • Schonbrunner, N.1    Pappenburger, G.2    Scharf, M.3    Engels, J.4    Kiefhaber, T.5
  • 17
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco, K. W., Simons, K. T., and Baker, D. (1998) Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277, 985-994.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 18
    • 0034652206 scopus 로고    scopus 로고
    • Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism
    • Fersht, A. R. (2000) Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism. Proc. Natl. Acad. Sci. U.S.A. 97, 1525-1529.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 1525-1529
    • Fersht, A.R.1
  • 19
    • 33947466111 scopus 로고
    • Theory of elastic mechanisms in fibrous proteins
    • Flory, P. J. (1956) Theory of elastic mechanisms in fibrous proteins. J. Am. Chem. Soc. 78, 5222-5235.
    • (1956) J. Am. Chem. Soc. , vol.78 , pp. 5222-5235
    • Flory, P.J.1
  • 20
    • 0023783477 scopus 로고
    • Conformational stability and activity of ribonuclease-T1 with zero, one, and two intact disulfide bonds
    • Pace, C. N., Grimsley, G. R., Thompson, J. A., and Barnett, B. J. (1988) Conformational stability and activity of ribonuclease-T1 with zero, one, and two intact disulfide bonds. J. Biol. Chem. 263, 11820-11825.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11820-11825
    • Pace, C.N.1    Grimsley, G.R.2    Thompson, J.A.3    Barnett, B.J.4
  • 21
  • 22
    • 0031919973 scopus 로고    scopus 로고
    • Evidence for barrier-limited protein folding kinetics on the microsecond time scale
    • Shastry, M. C. R., and Roder, H. (1998) Evidence for barrier-limited protein folding kinetics on the microsecond time scale. Nat. Struct. Biol. 5, 385-392.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 385-392
    • Shastry, M.C.R.1    Roder, H.2
  • 24
    • 0029000696 scopus 로고
    • Knowledge-based potentials for proteins
    • Sippl, M. J. (1995) Knowledge-based potentials for proteins. Curr. Opin. Struct. Biol. 5, 229-235.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 229-235
    • Sippl, M.J.1
  • 25
    • 0029919190 scopus 로고    scopus 로고
    • Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading
    • Miyazawa, S., and Jernigan, R. L. (1996) Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading. J. Mol. Biol. 256, 623-644.
    • (1996) J. Mol. Biol. , vol.256 , pp. 623-644
    • Miyazawa, S.1    Jernigan, R.L.2
  • 26
    • 0035342435 scopus 로고    scopus 로고
    • Ab initio protein structure prediction using physio-chemical potentials
    • Gibbs, N., Sessions, R. B., and Clarke, A. R. (2001) Ab initio protein structure prediction using physio-chemical potentials. Proteins: Struct., Funct., Genet. 43, 186-202.
    • (2001) Proteins: Struct., Funct., Genet. , vol.43 , pp. 186-202
    • Gibbs, N.1    Sessions, R.B.2    Clarke, A.R.3
  • 27
    • 0030937716 scopus 로고    scopus 로고
    • Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond
    • Mansfeld and Eijsink, V. G. (1997) Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond. J. Biol. Chem. 272, 11152-11156.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11152-11156
    • Mansfeld1    Eijsink, V.G.2
  • 28
    • 0024384198 scopus 로고
    • Protein engineering of disulfide bonds in subtilisin Bpn′
    • Mitchinson, C., and Wells, J. A. (1989) Protein engineering of disulfide bonds in subtilisin Bpn′. J. Biochem. 28, 4807-4815.
    • (1989) J. Biochem. , vol.28 , pp. 4807-4815
    • Mitchinson, C.1    Wells, J.A.2
  • 29
    • 0026059140 scopus 로고
    • Structure of domain-1 of rat lymphocyte-T CD2 antigen
    • Driscoll, P. C., Cyster, J. G., Campbell, I. D., and Williams (1991) Structure of domain-1 of rat lymphocyte-T CD2 antigen. Nature 353, 762-765.
    • (1991) Nature , vol.353 , pp. 762-765
    • Driscoll, P.C.1    Cyster, J.G.2    Campbell, I.D.3    Williams4
  • 30
    • 0031010678 scopus 로고    scopus 로고
    • Amide backbone and water-related H/D isotope effects on the dynamics of a protein folding reaction
    • Parker, M. J., and Clarke, A. R. (1997) Amide backbone and water-related H/D isotope effects on the dynamics of a protein folding reaction. Biochemistry 36, 5786-5794.
    • (1997) Biochemistry , vol.36 , pp. 5786-5794
    • Parker, M.J.1    Clarke, A.R.2
  • 32
    • 0028791393 scopus 로고
    • An integrated kinetic-analysis of intermediates and transition-states in protein-folding reactions
    • Parker, M. J., Spencer, J., and Clarke, A. R. (1995) An integrated kinetic-analysis of intermediates and transition-states in protein-folding reactions. J. Mol. Biol. 253, 771-786.
    • (1995) J. Mol. Biol. , vol.253 , pp. 771-786
    • Parker, M.J.1    Spencer, J.2    Clarke, A.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.