메뉴 건너뛰기




Volumn 12, Issue 4, 2010, Pages 961-982

Influence of conformational entropy on the protein folding rate

Author keywords

Conformational entropy; Energy of residue residue contacts; Folding rate; Native topology; Protein stability

Indexed keywords


EID: 77953492654     PISSN: None     EISSN: 10994300     Source Type: Journal    
DOI: 10.3390/e12040961     Document Type: Review
Times cited : (9)

References (73)
  • 1
    • 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, A.V.; Badretdinov, A.Ya. 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.Ya.2
  • 2
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • Jackson, S.E. How do small single-domain proteins fold? Fold. Des. 1998, 3, R81-R91.
    • (1998) Fold. Des. , vol.3
    • Jackson, S.E.1
  • 3
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco, K.W.; Simons, K.W.; 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.W.2    Baker, D.3
  • 4
    • 67849124732 scopus 로고    scopus 로고
    • Protein folding rates and stability: How much is there beyond size?
    • De Sancho, D.; Doshi, U.; Munoz, V. Protein folding rates and stability: How much is there beyond size? J. Am. Chem. Soc. 2009, 131, 2074-2075.
    • (2009) J Am. Chem. Soc. , vol.131 , pp. 2074-2075
    • De Sancho, D.1    Doshi, U.2    Munoz, V.3
  • 5
    • 0037402639 scopus 로고    scopus 로고
    • Chain length is the main determinant of the folding rate for proteins with three-state folding kinetics
    • Galzitskaya, O.V.; Garbuzynskiy, S.O.; Ivankov, D.N.; Finkelstein, A.V. Chain length is the main determinant of the folding rate for proteins with three-state folding kinetics. Proteins 2003, 51, 162-166.
    • (2003) Proteins , vol.51 , pp. 162-166
    • Galzitskaya, O.V.1    Garbuzynskiy, S.O.2    Ivankov, D.N.3    Finkelstein, A.V.4
  • 6
    • 0346458804 scopus 로고    scopus 로고
    • Class-Specific correlations between protein folding rate, structure-derived, and sequence-derived descriptors
    • Kuznetsov, I.B.; Rackovsky, S. Class-Specific correlations between protein folding rate, structure-derived, and sequence-derived descriptors. Proteins 2004, 54, 333-341.
    • (2004) Proteins , vol.54 , pp. 333-341
    • Kuznetsov, I.B.1    Rackovsky, S.2
  • 8
    • 0032570543 scopus 로고    scopus 로고
    • Folding kinetics of the SH3 domain of PI3 kinase by Real-Time NMR combined with optical spectroscopy
    • Guijarro, J.I.; Morton, C.J.; Plaxco, K.W.; Campbell, I.D.; Dobson, C.M. 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
  • 12
    • 0032529366 scopus 로고    scopus 로고
    • On the mechanism of human Stefin B folding: I. comparison to homologous Stefin A. influence of Ph and Trifluoroethanol on the fast and slow folding phases
    • Zerovnik, E.; Virden, R.; Jerala, R.; Turk, V.; Waltho, J.P. On the mechanism of human Stefin B folding: I. comparison to homologous Stefin A. influence of Ph and Trifluoroethanol on the fast and slow folding phases. Proteins 1998, 32, 296-303.
    • (1998) Proteins , vol.32 , pp. 296-303
    • Zerovnik, E.1    Virden, R.2    Jerala, R.3    Turk, V.4    Waltho, J.P.5
  • 13
    • 0000050196 scopus 로고
    • From minimal models to real proteins: Time Scales for Protein Folding Kinetics
    • Thirumalai, D. From minimal models to real proteins: Time Scales for Protein Folding Kinetics. J. Phys. Orsay Fr. 1995, 5, 1457-1467.
    • (1995) J. Phys. Orsay Fr. , vol.5 , pp. 1457-1467
    • Thirumalai, D.1
  • 15
    • 0031486612 scopus 로고    scopus 로고
    • Physical reasons for fast folding of stable spatial structure of proteins: A solution of the Levinthal Paradox
    • (Russia) Engl. Edition
    • Finkelstein, A.V.; Badretdinov, A.Ya. Physical reasons for fast folding of stable spatial structure of proteins: A solution of the Levinthal Paradox. Mol. Biol. (Russia) Engl. Edition 1997, 31, 391-398.
    • (1997) Mol. Biol. , vol.31 , pp. 391-398
    • Finkelstein, A.V.1    Badretdinov, A.Ya.2
  • 16
    • 0035850732 scopus 로고    scopus 로고
    • Roles of native topology and chain-length scaling in protein folding: A simulation study with a Gō-Like model
    • Koga, N.; Takada, S. Roles of native topology and chain-length scaling in protein folding: A simulation study with a Gō-Like model. J. Mol. Biol. 2001, 313, 171-180.
    • (2001) J. Mol. Biol. , vol.313 , pp. 171-180
    • Koga, N.1    Takada, S.2
  • 18
    • 68149142712 scopus 로고    scopus 로고
    • Coupling between properties of the protein shape and the rate of protein folding
    • Ivankov, D.N.; Bogatyreva, N.S.; Lobanov, M.Yu.; Galzitskaya, O.V. Coupling between properties of the protein shape and the rate of protein folding. PLoS ONE 2009, 4, e6476.
    • (2009) PLoS ONE , vol.4
    • Ivankov, D.N.1    Bogatyreva, N.S.2    Lobanov, M.Yu.3    Galzitskaya, O.V.4
  • 19
    • 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. 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
  • 21
    • 0037133574 scopus 로고    scopus 로고
    • How the folding rate constant of simple, single-domain proteins depends on the number of native contacts
    • Makarov, D.E.; Keller, C.A.; Plaxco, K.W.; Metiu, H. How the folding rate constant of simple, single-domain proteins depends on the number of native contacts. Proc. Natl. Acad. Sci. USA 2002, 9, 3535-3539.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.9 , pp. 3535-3539
    • Makarov, D.E.1    Keller, C.A.2    Plaxco, K.W.3    Metiu, H.4
  • 22
    • 17144369578 scopus 로고    scopus 로고
    • Protein folding rates estimated from contact predictions
    • Punta, M.; Rost, B. Protein folding rates estimated from contact predictions. J. Mol. Biol. 2005, 348, 507-512.
    • (2005) J. Mol. Biol. , vol.348 , pp. 507-512
    • Punta, M.1    Rost, B.2
  • 23
    • 0037432567 scopus 로고    scopus 로고
    • Local secondary structure content predicts folding rates for simple, two-state proteins
    • Gong, H.; Isom, D.G.; Srinivasan, R.; Rose, G.D. Local secondary structure content predicts folding rates for simple, two-state proteins. J. Mol. Biol. 2003, 327, 1149-1154.
    • (2003) J. Mol. Biol. , vol.327 , pp. 1149-1154
    • Gong, H.1    Isom, D.G.2    Srinivasan, R.3    Rose, G.D.4
  • 24
    • 0037566828 scopus 로고    scopus 로고
    • A simple parameter relating sequences with folding rates of small alpha helical proteins
    • Shao, H.; Peng, Y.; Zeng, Z.-H. A simple parameter relating sequences with folding rates of small alpha helical proteins. Protein Pept. Lett. 2003, 10, 277-280.
    • (2003) Protein Pept. Lett. , vol.10 , pp. 277-280
    • Shao, H.1    Peng, Y.2    Zeng, Z.-H.3
  • 25
    • 0038047129 scopus 로고    scopus 로고
    • Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding
    • Calloni, G.; Taddei, N.; Plaxco, K.W.; Ramponi, G.; Stefani, M.; Chiti, F. Comparison of the folding processes of distantly related proteins. Importance of hydrophobic content in folding. J. Mol. Biol. 2003, 330, 577-591.
    • (2003) J. Mol. Biol. , vol.330 , pp. 577-591
    • Calloni, G.1    Taddei, N.2    Plaxco, K.W.3    Ramponi, G.4    Stefani, M.5    Chiti, F.6
  • 26
    • 12944309313 scopus 로고    scopus 로고
    • Scaling of folding times with protein size
    • Naganathan, A.N.; Munoz, V. Scaling of folding times with protein size. J. Am. Chem. Soc. 2005, 127, 480-481.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 480-481
    • Naganathan, A.N.1    Munoz, V.2
  • 27
    • 0034028323 scopus 로고    scopus 로고
    • Optimal region of average side-chain entropy for fast protein folding
    • Galzitskaya, O.V.; Surin, A.K.; Nakamura, H. Optimal region of average side-chain entropy for fast protein folding. Protein Sci. 2000, 9, 580-586.
    • (2000) Protein Sci , vol.9 , pp. 580-586
    • Galzitskaya, O.V.1    Surin, A.K.2    Nakamura, H.3
  • 28
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A.G.; Brenner, S.E.; Hubbard, T.; Chothia, C. SCOP: A structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 1995, 247, 536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 29
    • 33645027665 scopus 로고    scopus 로고
    • Entropy capacity determines protein folding
    • Galzitskaya, O.V.; Garbuzynskiy, S.O. Entropy capacity determines protein folding. Proteins 2006, 63, 144-154.
    • (2006) Proteins , vol.63 , pp. 144-154
    • Galzitskaya, O.V.1    Garbuzynskiy, S.O.2
  • 32
    • 0016696599 scopus 로고
    • Studies on protein folding, unfolding and fluctuations by computer simulation I. The effect of specific amino acid sequence represented by specific inter-unit interactions
    • Taketomi, H.; Ueda, Y.; Gō, N. Studies on protein folding, unfolding and fluctuations by computer simulation. I. The effect of specific amino acid sequence represented by specific inter-unit interactions. Int. J. Pept. Protein Res. 1975, 7, 445-459.
    • (1975) Int. J. Pept. Protein Res. , vol.7 , pp. 445-459
    • Taketomi, H.1    Ueda, Y.2    Gō, N.3
  • 35
    • 0028958601 scopus 로고
    • Characterizing transition states in protein folding: An essential step in the puzzle
    • Fersht, A.R. Characterizing transition states in protein folding: An essential step in the puzzle. Curr. Opin. Struct. Biol. 1995, 5, 79-84.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 79-84
    • Fersht, A.R.1
  • 36
    • 0031043161 scopus 로고    scopus 로고
    • Nucleation mechanisms in protein folding
    • Fersht, A.R. Nucleation mechanisms in protein folding. Curr. Opin. Struct. Biol. 1997, 7, 3-9.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 3-9
    • Fersht, A.R.1
  • 37
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • Matouschek, J.T.; Kellis, J.T.Jr.; Serrano, L.; Fersht, A.R. Mapping the transition state and pathway of protein folding by protein engineering. Nature 1989, 340, 122-126.
    • (1989) Nature , vol.340 , pp. 122-126
    • Matouschek, J.T.1    Kellis J.T., Jr.2    Serrano, L.3    Fersht, A.R.4
  • 38
    • 0025698613 scopus 로고
    • Transient folding intermediates characterized by protein engineering
    • Matouschek, A.; Kellis, J.T.Jr.; Serrano, L.; Bycroft, M.; Fersht, A.R. Transient folding intermediates characterized by protein engineering. Nature 1990, 346, 440-445.
    • (1990) Nature , vol.346 , pp. 440-445
    • Matouschek, A.1    Kellis J.T., Jr.2    Serrano, L.3    Bycroft, M.4    Fersht, A.R.5
  • 39
    • 0026511656 scopus 로고
    • The folding of an enzyme I. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht, A.R.; Matouschek, A.; Serrano, L. The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 1992, 224, 771-782.
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 40
    • 0028024928 scopus 로고
    • Specific nucleus as a transition state for protein folding: an evidence from lattice model
    • Abkevich, V.I.; Gutin, A.M.; Shakhnovich, E.I. Specific nucleus as a transition state for protein folding: an evidence from lattice model. Biochemistry 1994, 33, 10026-10036.
    • (1994) Biochemistry , vol.33 , pp. 10026-10036
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 41
    • 0030979740 scopus 로고    scopus 로고
    • Folding funnels and energy landscapes of larger proteins within the capillarity approximation
    • Wolynes, P.G. Folding funnels and energy landscapes of larger proteins within the capillarity approximation. Proc. Natl. Acad. Sci. USA 1997, 94, 6170-6175.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6170-6175
    • Wolynes, P.G.1
  • 42
    • 0026665778 scopus 로고
    • Side-chain entropy opposes alpha-Helix formation but rationalizes experimentally determined Helix-forming propensities
    • Creamer, T.P.; Rose, G.D. Side-chain entropy opposes alpha-Helix formation but rationalizes experimentally determined Helix-forming propensities. Proc. Natl. Acad. Sci. USA 1992, 89, 5937-5941.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5937-5941
    • Creamer, T.P.1    Rose, G.D.2
  • 43
    • 0031214818 scopus 로고    scopus 로고
    • Folding and stability of a fibronectin type III domain of human tenascin
    • Clarke, J.; Hamill, S.J.; Johnson, C.M. Folding and stability of a fibronectin type III 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
  • 44
    • 0033957144 scopus 로고    scopus 로고
    • Folding of beta-sandwich proteins: Three-state transition of a Fibronectin type III module
    • Cota, E.; Clarke, J. Folding of beta-sandwich proteins: Three-state transition of a Fibronectin type III module. Protein Sci. 2000, 9, 112-120.
    • (2000) Protein Sci , vol.9 , pp. 112-120
    • Cota, E.1    Clarke, J.2
  • 45
    • 0032570543 scopus 로고    scopus 로고
    • Folding kinetics of the SH3 domain of PI3 kinase by Real-Time NMR combined with optical spectroscopy
    • Guijarro, J.I.; Morton, C.J.; Plaxco, K.W.; Campbell, I.D.; Dobson, C.M. 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
  • 46
    • 0031444104 scopus 로고    scopus 로고
    • Folding dynamics of the Src SH3 domain
    • Grantcharova, V.P.; Baker, D. Folding dynamics of the Src SH3 domain. Biochemistry 1997, 36, 15685-15692.
    • (1997) Biochemistry , vol.36 , pp. 15685-15692
    • Grantcharova, V.P.1    Baker, D.2
  • 50
    • 0030750236 scopus 로고    scopus 로고
    • High-energy channeling in protein folding
    • Silow, M.; Oliveberg, M. High-energy channeling in protein folding. Biochemistry 1997, 36, 7633-7637.
    • (1997) Biochemistry , vol.36 , pp. 7633-7637
    • Silow, M.1    Oliveberg, M.2
  • 51
    • 79251474677 scopus 로고    scopus 로고
    • Estimation of protein folding rate from Monte-Carlo simulations and entropy capacity
    • press
    • Galzitskaya, O.V. Estimation of protein folding rate from Monte-Carlo simulations and entropy capacity. Curr. Protein Pept. Sci. In press.
    • Curr. Protein Pept. Sci.
    • Galzitskaya, O.V.1
  • 54
    • 15544390249 scopus 로고    scopus 로고
    • Protein structure and evolutionary history determine sequence space topology
    • Shakhnovich, B.E.; Deeds, E.; Delisi, C.; Shakhnovich, E. Protein structure and evolutionary history determine sequence space topology. Genome. Res. 2005, 15, 385-392.
    • (2005) Genome. Res. , vol.15 , pp. 385-392
    • Shakhnovich, B.E.1    Deeds, E.2    Delisi, C.3    Shakhnovich, E.4
  • 55
    • 0041305985 scopus 로고    scopus 로고
    • Natural selection of more designable folds: A mechanism for thermophilic adaptation
    • England, J.L.; Shakhnovich, B.E.; Shakhnovich, E.I. Natural selection of more designable folds: A mechanism for thermophilic adaptation. Proc. Natl. Acad. Sci. USA 2003, 100, 8727-8731.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8727-8731
    • England, J.L.1    Shakhnovich, B.E.2    Shakhnovich, E.I.3
  • 56
    • 0032493479 scopus 로고    scopus 로고
    • Solution structure of the B-Myb DNA-binding domain: A possible role for conformational instability of the protein in DNA binding and control of gene expression
    • McIntosh, P.B.; Frenkiel, T.A.; Wollborn, U.; McCormick, J.E.; Klempnauer, K.H.; Feeney, J.; Carr, M.D. Solution structure of the B-Myb DNA-binding domain: A possible role for conformational instability of the protein in DNA binding and control of gene expression. Biochemistry 1998, 37, 9619-9629.
    • (1998) Biochemistry , vol.37 , pp. 9619-9629
    • McIntosh, P.B.1    Frenkiel, T.A.2    Wollborn, U.3    McCormick, J.E.4    Klempnauer, K.H.5    Feeney, J.6    Carr, M.D.7
  • 57
    • 0032967237 scopus 로고    scopus 로고
    • The solution structure of the homeodomain of the rat insulin-gene enhancer protein Isl-1 Comparison with other homeodomains
    • Ippel, H.; Larsson, G.; Behravan, G.; Zdunek, J.; Lundqvist, M.; Schleucher, J.; Lycksell, P.O.; Wijmenga, S. The solution structure of the homeodomain of the rat insulin-gene enhancer protein Isl-1. Comparison with other homeodomains. J. Mol. Biol. 1999, 288, 689-703.
    • (1999) J. Mol. Biol. , vol.288 , pp. 689-703
    • Ippel, H.1    Larsson, G.2    Behravan, G.3    Zdunek, J.4    Lundqvist, M.5    Schleucher, J.6    Lycksell, P.O.7    Wijmenga, S.8
  • 58
    • 0031790334 scopus 로고    scopus 로고
    • Metastable states and folding free energy barriers
    • Baker, D. Metastable states and folding free energy barriers. Nature Struct. Biol. 1998, 5, 1021-1024.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 1021-1024
    • Baker, D.1
  • 59
    • 0032558779 scopus 로고    scopus 로고
    • Unfolded conformations of α-Lytic protease are more stable than its native state
    • Sohl, J.L.; Jaswal, S.S.; Agard, D.A. Unfolded conformations of α-Lytic protease are more stable than its native state. Nature 1998, 395, 817-819.
    • (1998) Nature , vol.395 , pp. 817-819
    • Sohl, J.L.1    Jaswal, S.S.2    Agard, D.A.3
  • 61
    • 0033605278 scopus 로고    scopus 로고
    • Prion domain initiation of amyloid formation in vitro from native Ure2p
    • Taylor, K.L.; Cheng, N.; Williams, R.W.; Steven, A.C.; Wickner, R.B. Prion domain initiation of amyloid formation in vitro from native Ure2p. Science 1999, 283, 1339-1343.
    • (1999) Science , vol.283 , pp. 1339-1343
    • Taylor, K.L.1    Cheng, N.2    Williams, R.W.3    Steven, A.C.4    Wickner, R.B.5
  • 62
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Reassessing the protein structure-function paradigm
    • Wright, P.E.; Dyson, H.J. Intrinsically unstructured proteins: Reassessing the protein structure-function paradigm. J. Mol. Biol. 1999, 293, 321-331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 63
    • 22744437069 scopus 로고    scopus 로고
    • Natively disordered proteins: Functions and predictions
    • Romero, P.; Obradovic, Z.; Dunker, A.K. Natively disordered proteins: Functions and predictions. Appl. Bioinformatics 2004, 3, 105-113.
    • (2004) Appl. Bioinformatics , vol.3 , pp. 105-113
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 64
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink, A.L. Natively unfolded proteins. Curr. Opin. Struct. Biol. 2005, 15, 35-41.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 65
    • 27144464910 scopus 로고    scopus 로고
    • Flexible Nets. The roles of intrinsic disorder in protein interaction networks
    • Dunker, A.K.; Cortese, M.S.; Romero, P.; Iakoucheva, L.M.; Uversky, V.N. Flexible Nets. The roles of intrinsic disorder in protein interaction networks. FEBS J. 2005, 272, 5129-5148.
    • (2005) FEBS J , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 67
    • 33751381791 scopus 로고    scopus 로고
    • FoldUnfold: web server for the prediction of disordered regions in protein chain
    • Galzitskaya, O.V.; Garbuzynskiy, S.O.; Lobanov, M.Y. FoldUnfold: web server for the prediction of disordered regions in protein chain. Bioinformatics 2006, 22, 2948-2949.
    • (2006) Bioinformatics , vol.22 , pp. 2948-2949
    • Galzitskaya, O.V.1    Garbuzynskiy, S.O.2    Lobanov, M.Y.3
  • 68
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H.J.; Wright, P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell. Biol. 2005, 6, 197-208.
    • (2005) Nat. Rev. Mol. Cell. Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 69
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn, O.B. Molten globule and protein folding. Adv. Protein Chem. 1995, 47, 83-229.
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 71
    • 0033582587 scopus 로고    scopus 로고
    • Thermodynamics of model prions and its implications for the problem of prion protein folding
    • Harrison, P.M.; Chan, H.S.; Prusiner, S.B.; Cohen, F.E. Thermodynamics of model prions and its implications for the problem of prion protein folding. J. Mol. Biol. 1999, 286, 593-606.
    • (1999) J. Mol. Biol. , vol.286 , pp. 593-606
    • Harrison, P.M.1    Chan, H.S.2    Prusiner, S.B.3    Cohen, F.E.4
  • 72
    • 0042847751 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
    • Jimenez, J.L.; Guijarro, J.I.; Orlova, E.; Zurdo, J.; Dobson, C.M.; Sunde, M.; Saibil, H.R. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 1999, 18, 815-821.
    • (1999) EMBO J , vol.18 , pp. 815-821
    • Jimenez, J.L.1    Guijarro, J.I.2    Orlova, E.3    Zurdo, J.4    Dobson, C.M.5    Sunde, M.6    Saibil, H.R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.