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Volumn 58, Issue 2, 2005, Pages 389-395

Topological determinants of protein unfolding rates

Author keywords

Clustering coefficient; Contact order; Folding unfolding rate; Impact of edge removal; Protein folding; Protein structure

Indexed keywords

PEPTIDES AND PROTEINS; PROTEIN ALPHA; PROTEIN ALPHABETA; PROTEIN BETA; PROTEIN BETA SANDWICH; UNCLASSIFIED DRUG;

EID: 11344269939     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20324     Document Type: Article
Times cited : (21)

References (41)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C. Principles that govern the folding of protein chains. Science 1973;181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.1
  • 3
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal C. Are there pathways for protein folding? J Chem Phys 1968;65:44-45.
    • (1968) J Chem Phys , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 7
    • 0030979740 scopus 로고    scopus 로고
    • Folding funnels and energy landscapes of larger proteins within the capillarity approximations
    • Wolynes PG. Folding funnels and energy landscapes of larger proteins within the capillarity approximations. Proc Natl Acad Sci USA 1997;94:6170-6175.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6170-6175
    • Wolynes, P.G.1
  • 8
    • 0030623529 scopus 로고    scopus 로고
    • Rate of protein folding near the point of thermodynamic equilibrium between the coil and the most stable chain fold
    • Finkelstein AV, Badretdinov AY. Rate of protein folding near the point of thermodynamic equilibrium between the coil and the most stable chain fold. Fold Des 1997;2:115-121.
    • (1997) Fold des , vol.2 , pp. 115-121
    • Finkelstein, A.V.1    Badretdinov, A.Y.2
  • 9
    • 0030443105 scopus 로고    scopus 로고
    • Factors governing the foldability of proteins
    • Kilmov DK, Thirumalai D. Factors governing the foldability of proteins. Proteins 1997;26:411-441.
    • (1997) Proteins , vol.26 , pp. 411-441
    • Kilmov, D.K.1    Thirumalai, D.2
  • 11
    • 0026019655 scopus 로고
    • Rate of beta-structure formation in polypeptides
    • Finkelstein AV. Rate of beta-structure formation in polypeptides. Proteins 1991;9:23-27.
    • (1991) Proteins , vol.9 , pp. 23-27
    • Finkelstein, A.V.1
  • 13
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson JD, Onuchic JN, Socci ND, Wolynes PG. Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins 1995;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
  • 15
    • 0030628053 scopus 로고    scopus 로고
    • On the theory of folding kinetics for short proteins
    • Pande VS, Grosberg AY, Tanaka T. On the theory of folding kinetics for short proteins. Fold Des 1997;2:109-114.
    • (1997) Fold des , vol.2 , pp. 109-114
    • Pande, V.S.1    Grosberg, A.Y.2    Tanaka, T.3
  • 16
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • Jackson SE. How do small single-domain proteins fold? Fold Des 1998;3:R81-R91.
    • (1998) Fold des , vol.3
    • Jackson, S.E.1
  • 17
    • 0028935887 scopus 로고
    • Structure and stability of monomeric gamma represser: NMR evidence for two-state folding
    • Huang GS, Oas TG. Structure and stability of monomeric gamma represser: NMR evidence for two-state folding. Biochemistry 1995;34:3884-3892.
    • (1995) Biochemistry , vol.34 , pp. 3884-3892
    • Huang, G.S.1    Oas, T.G.2
  • 20
    • 0029965111 scopus 로고    scopus 로고
    • Fast and one-step folding for closely and distantly related homologous proteins of a four-bundle family
    • Kragelund BB, Poulsen FM. Fast and one-step folding for closely and distantly related homologous proteins of a four-bundle family. J Mol Biol 1996;256:187-200.
    • (1996) J Mol Biol , vol.256 , pp. 187-200
    • Kragelund, B.B.1    Poulsen, F.M.2
  • 21
    • 0031047914 scopus 로고    scopus 로고
    • Submillisecond protein folding kinetics studied by ultrarapid mixing
    • Chan CK, Hofrichter J. Submillisecond protein folding kinetics studied by ultrarapid mixing. Proc Natl Acad Sci USA 1997;94:1779-1784.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1779-1784
    • Chan, C.K.1    Hofrichter, J.2
  • 23
    • 0028331876 scopus 로고
    • Thermodynamic and kinetic-ananlysis of the SH3 domain of spectrin shows a 2-state folding transition
    • Viguera AR, Martinez J, Fillmonov V, Mateo P, Serrano L. Thermodynamic and kinetic-ananlysis of the SH3 domain of spectrin shows a 2-state folding transition. Biochemistry 1994;33:2142-2150.
    • (1994) Biochemistry , vol.33 , pp. 2142-2150
    • Viguera, A.R.1    Martinez, J.2    Fillmonov, V.3    Mateo, P.4    Serrano, L.5
  • 24
    • 0029760326 scopus 로고    scopus 로고
    • Different folding transition-state may result in the same native structure
    • Viguera AR, Serrano L, Wilmanns M. Different folding transition-state may result in the same native structure. Nat Struct Biol 1996;3:874-880.
    • (1996) Nat Struct Biol , vol.3 , pp. 874-880
    • Viguera, A.R.1    Serrano, L.2    Wilmanns, M.3
  • 25
    • 0031444104 scopus 로고    scopus 로고
    • Folding dynamcis of the src SH3 domain
    • Grantcharova VP, Baker D. Folding dynamcis of the src SH3 domain. Biochemistry 1997;36:15685-15692.
    • (1997) Biochemistry , vol.36 , pp. 15685-15692
    • Grantcharova, V.P.1    Baker, D.2
  • 26
    • 0032570543 scopus 로고    scopus 로고
    • Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy
    • Guijarro JI, Morton CJ, Plaxco KW, Campbell ID, Dobson CM. Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy. J Mol Biol 1998;276:657-667.
    • (1998) J Mol Biol , vol.276 , pp. 657-667
    • Guijarro, J.I.1    Morton, C.J.2    Plaxco, K.W.3    Campbell, I.D.4    Dobson, C.M.5
  • 27
    • 0032562182 scopus 로고    scopus 로고
    • The folding kinetics and thermodynamics of the Fyn-SH3 domain
    • Plaxco KW, Dobson CM. The folding kinetics and thermodynamics of the Fyn-SH3 domain. Biochemistry 1998;37:2529-2537.
    • (1998) Biochemistry , vol.37 , pp. 2529-2537
    • Plaxco, K.W.1    Dobson, C.M.2
  • 28
    • 0033548553 scopus 로고    scopus 로고
    • Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9
    • Ferguson N, Capaldi AP, James R, Kleanthous C, Radford SE. Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9. J Mol Biol 1999;286:1597-1608.
    • (1999) J Mol Biol , vol.286 , pp. 1597-1608
    • Ferguson, N.1    Capaldi, A.P.2    James, R.3    Kleanthous, C.4    Radford, S.E.5
  • 29
    • 0031214818 scopus 로고    scopus 로고
    • Folding and stability of a fibronectin type3 domain of human tenascin
    • Clarke J, Hamill SJ, Johnson CM. Folding and stability of a fibronectin type3 domain of human tenascin. J Mol Biol 1997;270:771-778.
    • (1997) J Mol Biol , vol.270 , pp. 771-778
    • Clarke, J.1    Hamill, S.J.2    Johnson, C.M.3
  • 30
    • 0033200251 scopus 로고    scopus 로고
    • Folding studies of immunoglobuline-like beta-sandwich proteins suggest that they share a common folding pathway
    • Clarke J, Cota E, Fowler SB, Hamill SJ. Folding studies of immunoglobuline-like beta-sandwich proteins suggest that they share a common folding pathway. Structure 1999;7:1145-1153.
    • (1999) Structure , vol.7 , pp. 1145-1153
    • Clarke, J.1    Cota, E.2    Fowler, S.B.3    Hamill, S.J.4
  • 31
    • 0028788480 scopus 로고
    • Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2
    • Villegas V, Azuaga A, Catasus LI, Reverter D, Mateo PL, Aviles FX, Serrano L. Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2. Biochemistry 1995;34:15105-15110.
    • (1995) Biochemistry , vol.34 , pp. 15105-15110
    • Villegas, V.1    Azuaga, A.2    Catasus, L.I.3    Reverter, D.4    Mateo, P.L.5    Aviles, F.X.6    Serrano, L.7
  • 34
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco KW, Simons KT, Baker D. Contact order, transition state placement and the refolding rates of single domain proteins. J Mol Biol 1998;277:985-994.
    • (1998) J Mol Biol , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 35
    • 0034687123 scopus 로고    scopus 로고
    • Topology, stability, sequence, and length: Defining the determinants of two-state protein folding kinetics
    • Plaxco KW, Simons KT, Ruczinski I, Baker D. Topology, stability, sequence, and length: defining the determinants of two-state protein folding kinetics. Biochemistry 2000;39:11177-11183.
    • (2000) Biochemistry , vol.39 , pp. 11177-11183
    • Plaxco, K.W.1    Simons, K.T.2    Ruczinski, I.3    Baker, D.4
  • 36
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • Baker D. A surprising simplicity to protein folding. Nature 2000;405:39-42.
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 37
    • 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 AR. 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 USA 2000;97:1525-1529.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1525-1529
    • Fersht, A.R.1
  • 39
    • 0035252350 scopus 로고    scopus 로고
    • Three key residues from a critical contact network in a protein folding transition state
    • Bendruscolo M, Paci E, Dobson CM, Karplus M. Three key residues from a critical contact network in a protein folding transition state. Nature 2001;409:641-645.
    • (2001) Nature , vol.409 , pp. 641-645
    • Bendruscolo, M.1    Paci, E.2    Dobson, C.M.3    Karplus, M.4
  • 40
    • 0032482432 scopus 로고    scopus 로고
    • Dynamics of "Small-World" networks
    • Watts DJ, Strogatz SH. Dynamics of "Small-World" networks. Nature 1998;393:440-442.
    • (1998) Nature , vol.393 , pp. 440-442
    • Watts, D.J.1    Strogatz, S.H.2
  • 41
    • 0034721164 scopus 로고    scopus 로고
    • Error and attack tolerance of complex networks
    • Albert R, Jeong H, Barabasi AL. Error and attack tolerance of complex networks. Nature 2000;406:378-381.
    • (2000) Nature , vol.406 , pp. 378-381
    • Albert, R.1    Jeong, H.2    Barabasi, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.