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Volumn 5, Issue 11, 2010, Pages

Nonnative interactions in coupled folding and binding processes of intrinsically disordered proteins

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN;

EID: 78149492409     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0015375     Document Type: Article
Times cited : (39)

References (79)
  • 1
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill KA, Chan HS (1997) From Levinthal to pathways to funnels. Nat Struct Biol 4: 10-19.
    • (1997) Nat Struct Biol , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 2
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson JD, Onuchic JN, Socci ND, Wolynes PG (1995) Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins 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
  • 3
    • 0033056708 scopus 로고    scopus 로고
    • Folding funnels, binding funnels, and protein function
    • Tsai CJ, Kumar S, Ma BY, Nussinov R (1999) Folding funnels, binding funnels, and protein function. Protein Sci 8: 1181-1190.
    • (1999) Protein Sci , vol.8 , pp. 1181-1190
    • Tsai, C.J.1    Kumar, S.2    Ma, B.Y.3    Nussinov, R.4
  • 4
    • 0017842051 scopus 로고
    • Studies on protein folding, unfolding, and fluctuations by computer simulation. II. A. three-dimensional lattice model of lysozyme
    • Ueda Y, Taketomi H, Gō N (1978) Studies on protein folding, unfolding, and fluctuations by computer simulation. II. A. three-dimensional lattice model of lysozyme. Biopolymers 17: 1531-1548.
    • (1978) Biopolymers , vol.17 , pp. 1531-1548
    • Ueda, Y.1    Taketomi, H.2    Gō, N.3
  • 5
    • 0020972782 scopus 로고
    • Theoretical studies of protein folding
    • Gō N (1983) Theoretical studies of protein folding. Annu Rev Biophys Bioeng 12: 183-210.
    • (1983) Annu Rev Biophys Bioeng , vol.12 , pp. 183-210
    • Gō, N.1
  • 6
    • 18344391877 scopus 로고    scopus 로고
    • Protein structures and optimal folding from a geometrical variational principle
    • Micheletti C, Banavar JR, Maritan A, Seno F (1999) Protein structures and optimal folding from a geometrical variational principle. Phys Rev Lett 82: 3372-3375.
    • (1999) Phys Rev Lett , vol.82 , pp. 3372-3375
    • Micheletti, C.1    Banavar, J.R.2    Maritan, A.3    Seno, F.4
  • 7
    • 0034685604 scopus 로고    scopus 로고
    • Topological and energetic factors: What determines the structural details of the transition state ensemble and "enroute" intermediates for protein folding? An investigation for small globular proteins
    • Clementi C, Nymeyer H, Onuchic JN (2000) Topological and energetic factors: what determines the structural details of the transition state ensemble and "enroute" intermediates for protein folding? An investigation for small globular proteins. J Mol Biol 298: 937-953.
    • (2000) J Mol Biol , vol.298 , pp. 937-953
    • Clementi, C.1    Nymeyer, H.2    Onuchic, J.N.3
  • 8
    • 19444384541 scopus 로고    scopus 로고
    • Desolvation is a likely origin of robust enthalpic barriers to protein folding
    • Liu ZR, Chan HS (2005) Desolvation is a likely origin of robust enthalpic barriers to protein folding. J Mol Biol 349: 872-889.
    • (2005) J Mol Biol , vol.349 , pp. 872-889
    • Liu, Z.R.1    Chan, H.S.2
  • 9
    • 13444301037 scopus 로고    scopus 로고
    • A survey of flexible protein binding mechanisms and their transition states using native topology based energy landscapes
    • Levy Y, Cho SS, Onuchic JN, Wolynes PG (2005) A survey of flexible protein binding mechanisms and their transition states using native topology based energy landscapes. J Mol Biol 346: 1121-1145.
    • (2005) J Mol Biol , vol.346 , pp. 1121-1145
    • Levy, Y.1    Cho, S.S.2    Onuchic, J.N.3    Wolynes, P.G.4
  • 10
    • 77049109643 scopus 로고    scopus 로고
    • Folding simulations of a de novo designed protein with a bab fold
    • Qi YF, Huang YQ, Liang HH, Liu ZR, Lai LH (2010) Folding simulations of a de novo designed protein with a bab fold. Biophys J 98: 321-329.
    • (2010) Biophys J , vol.98 , pp. 321-329
    • Qi, Y.F.1    Huang, Y.Q.2    Liang, H.H.3    Liu, Z.R.4    Lai, L.H.5
  • 11
    • 1942521649 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of non-native interactions in protein folding: A single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state
    • Cho J-H, Sato S, Raleigh DP (2004) Thermodynamics and kinetics of non-native interactions in protein folding: a single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state. J Mol Biol 338: 827-837.
    • (2004) J Mol Biol , vol.338 , pp. 827-837
    • Cho, J.-H.1    Sato, S.2    Raleigh, D.P.3
  • 12
    • 25144470141 scopus 로고    scopus 로고
    • Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins
    • Cho J-H, Raleigh DP (2005) Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins. J Mol Biol 353: 174-185.
    • (2005) J Mol Biol , vol.353 , pp. 174-185
    • Cho, J.-H.1    Raleigh, D.P.2
  • 13
    • 0036183221 scopus 로고    scopus 로고
    • Im7 folding mechanism: Misfolding on a path to the native state
    • Capaldi AP, Kleanthous C, Radford SE (2002) Im7 folding mechanism: misfolding on a path to the native state. Nat Struct Biol 9: 209-216.
    • (2002) Nat Struct Biol , vol.9 , pp. 209-216
    • Capaldi, A.P.1    Kleanthous, C.2    Radford, S.E.3
  • 14
    • 27544451147 scopus 로고    scopus 로고
    • Antagonism, non-native interactions and non-two-state folding in S6 revealed by double-mutant cycle analysis
    • Otzen D (2005) Antagonism, non-native interactions and non-two-state folding in S6 revealed by double-mutant cycle analysis. Protein Eng Des Sel 18: 547-557.
    • (2005) Protein Eng Des Sel , vol.18 , pp. 547-557
    • Otzen, D.1
  • 15
    • 33750004434 scopus 로고    scopus 로고
    • Identification of a collapsed intermediate with non-native long-range interactions on the folding pathway of a pair of Fyn SH3 domain mutants by NMR relaxation dispersion spectroscopy
    • Neudecker P, Zarrine-Afsar A, Choy W-Y, Muhandiram DR, Davidson AR, et al. (2006) Identification of a collapsed intermediate with non-native long-range interactions on the folding pathway of a pair of Fyn SH3 domain mutants by NMR relaxation dispersion spectroscopy. J Mol Biol 363: 958-976.
    • (2006) J Mol Biol , vol.363 , pp. 958-976
    • Neudecker, P.1    Zarrine-Afsar, A.2    Choy, W.-Y.3    Muhandiram, D.R.4    Davidson, A.R.5
  • 16
    • 34447261443 scopus 로고    scopus 로고
    • The effect of increasing the stability of non-native interactions on the folding landscape of the bacterial immunity protein Im9
    • Morton VL, Friel CT, Allen LR, Paci E, Radford SE (2007) The effect of increasing the stability of non-native interactions on the folding landscape of the bacterial immunity protein Im9. J Mol Biol 371: 554-568.
    • (2007) J Mol Biol , vol.371 , pp. 554-568
    • Morton, V.L.1    Friel, C.T.2    Allen, L.R.3    Paci, E.4    Radford, S.E.5
  • 17
    • 0029904097 scopus 로고    scopus 로고
    • Role of non-native aromatic and hydrophobic interactions in the folding of hen egg white lysozyme
    • Rothwarf DM, Scheraga HA (1996) Role of non-native aromatic and hydrophobic interactions in the folding of hen egg white lysozyme. Biochemistry 35: 13797-13807.
    • (1996) Biochemistry , vol.35 , pp. 13797-13807
    • Rothwarf, D.M.1    Scheraga, H.A.2
  • 19
    • 0030623419 scopus 로고    scopus 로고
    • Role of a nonnative interaction in the folding of the protein G B1 domain as inferred from the conformational analysis of the a-helix fragment
    • Blanco FJ, Ortiz AR, Serrano L (1997) Role of a nonnative interaction in the folding of the protein G B1 domain as inferred from the conformational analysis of the a-helix fragment. Fold Des 2: 123-133.
    • (1997) Fold Des , vol.2 , pp. 123-133
    • Blanco, F.J.1    Ortiz, A.R.2    Serrano, L.3
  • 20
    • 0037117477 scopus 로고    scopus 로고
    • Unspecific hydrophobic stabilization of folding transition states
    • Viguera AR, Vega C, Serrano L (2002) Unspecific hydrophobic stabilization of folding transition states. Proc Natl Acad Sci USA 99: 5349-5354.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5349-5354
    • Viguera, A.R.1    Vega, C.2    Serrano, L.3
  • 21
  • 22
    • 0038461959 scopus 로고    scopus 로고
    • Rapid formation of non-native contacts during the folding of HPr revealed by real-time photo-CIDNP NMR and stopped-flow fluorescence experiments
    • Canet D, Lyon CE, Scheek RM, Robillard GT, Dobson CM, et al. (2003) Rapid formation of non-native contacts during the folding of HPr revealed by real-time photo-CIDNP NMR and stopped-flow fluorescence experiments. J Mol Biol 330: 397-407.
    • (2003) J Mol Biol , vol.330 , pp. 397-407
    • Canet, D.1    Lyon, C.E.2    Scheek, R.M.3    Robillard, G.T.4    Dobson, C.M.5
  • 23
    • 71149087504 scopus 로고    scopus 로고
    • Transient nonnative hydrogen bonds promote activation of a signaling protein
    • Gardino AK, Villali J, Kivenson A, Lei M, Liu CF, et al. (2009) Transient nonnative hydrogen bonds promote activation of a signaling protein. Cell 139: 1109-1118.
    • (2009) Cell , vol.139 , pp. 1109-1118
    • Gardino, A.K.1    Villali, J.2    Kivenson, A.3    Lei, M.4    Liu, C.F.5
  • 24
    • 26944492613 scopus 로고    scopus 로고
    • How do biomolecular systems speed up and regulate rates?
    • Zhou H-X (2005) How do biomolecular systems speed up and regulate rates? Phys Biol 2: R1-R25.
    • (2005) Phys Biol , vol.2
    • Zhou, H.-X.1
  • 25
    • 33751086423 scopus 로고    scopus 로고
    • Visualization of transient encounter complexes in protein-protein association
    • Tang C, Iwahara J, Clore GM (2006) Visualization of transient encounter complexes in protein-protein association. Nature 444: 383-386.
    • (2006) Nature , vol.444 , pp. 383-386
    • Tang, C.1    Iwahara, J.2    Clore, G.M.3
  • 26
    • 34250821717 scopus 로고    scopus 로고
    • Mechanism of coupled folding and binding of an intrinsically disordered protein
    • Sugase K, Dyson HJ, Wright PE (2007) Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature 447: 1021-1025.
    • (2007) Nature , vol.447 , pp. 1021-1025
    • Sugase, K.1    Dyson, H.J.2    Wright, P.E.3
  • 28
    • 0036928148 scopus 로고    scopus 로고
    • Validity of Gōmodels: Comparison with a solvent-shielded empirical energy decomposition
    • Paci E, Vendruscolo M, Karplus M (2002) Validity of Gōmodels: comparison with a solvent-shielded empirical energy decomposition. Biophys J 83: 3032-3038.
    • (2002) Biophys J , vol.83 , pp. 3032-3038
    • Paci, E.1    Vendruscolo, M.2    Karplus, M.3
  • 29
    • 77953569948 scopus 로고    scopus 로고
    • Roles of non-native hydrogen-bonding interaction in helix-coil transition of a single polypeptide as revealed by comparison between Gō-like and non-Gō models
    • Chen YT, Ding JD (2010) Roles of non-native hydrogen-bonding interaction in helix-coil transition of a single polypeptide as revealed by comparison between Gō-like and non-Gō models. Proteins 78: 2090-2100.
    • (2010) Proteins , vol.78 , pp. 2090-2100
    • Chen, Y.T.1    Ding, J.D.2
  • 30
    • 24144487130 scopus 로고    scopus 로고
    • Detection of non-native hydrophobic interactions in the denatured state of lysozyme by molecular dynamics simulations
    • Paci E, Vendruscolo M (2005) Detection of non-native hydrophobic interactions in the denatured state of lysozyme by molecular dynamics simulations. J Phys: Condens Matter 17: S1617-S1626.
    • (2005) J Phys: Condens Matter , vol.17
    • Paci, E.1    Vendruscolo, M.2
  • 31
    • 0029806946 scopus 로고    scopus 로고
    • Perturbations of the denatured state ensemble: Modeling their effects on protein stability and folding kinetics
    • Wrabl JO, Shortle D (1996) Perturbations of the denatured state ensemble: modeling their effects on protein stability and folding kinetics. Protein Sci 5: 2343-2352.
    • (1996) Protein Sci , vol.5 , pp. 2343-2352
    • Wrabl, J.O.1    Shortle, D.2
  • 32
    • 0034112774 scopus 로고    scopus 로고
    • Kinetics, thermodynamics and evolution of non-native interactions in a protein folding nucleus
    • Li L, Mirny LA, Shakhnovich EI (2000) Kinetics, thermodynamics and evolution of non-native interactions in a protein folding nucleus. Nat Struct Biol 7: 336-342.
    • (2000) Nat Struct Biol , vol.7 , pp. 336-342
    • Li, L.1    Mirny, L.A.2    Shakhnovich, E.I.3
  • 33
    • 3042677501 scopus 로고    scopus 로고
    • The effects of nonnative interactions on protein folding rates: Theory and simulation
    • Clementi C, Plotkin SS (2004) The effects of nonnative interactions on protein folding rates: theory and simulation. Protein Sci 13: 1750-1766.
    • (2004) Protein Sci , vol.13 , pp. 1750-1766
    • Clementi, C.1    Plotkin, S.S.2
  • 34
    • 0035576033 scopus 로고    scopus 로고
    • Speeding protein folding beyond the Gōmodel: How a little frustration sometimes helps
    • Plotkin SS (2001) Speeding protein folding beyond the Gōmodel: how a little frustration sometimes helps. Proteins 45: 337-345.
    • (2001) Proteins , vol.45 , pp. 337-345
    • Plotkin, S.S.1
  • 35
    • 0043094427 scopus 로고    scopus 로고
    • Folding of lattice protein chains with modified Gōpotential
    • Fan K, Wang J, Wang W (2002) Folding of lattice protein chains with modified Gōpotential. Eur Phys J B 30: 381-391.
    • (2002) Eur Phys J B , vol.30 , pp. 381-391
    • Fan, K.1    Wang, J.2    Wang, W.3
  • 36
    • 0036870910 scopus 로고    scopus 로고
    • The range of the contact interactions and the kinetics of the Go models of proteins
    • Cieplak M, Hoang TX (2002) The range of the contact interactions and the kinetics of the Go models of proteins. Int J Mod Phys C 13: 1231-1242.
    • (2002) Int J Mod Phys C , vol.13 , pp. 1231-1242
    • Cieplak, M.1    Hoang, T.X.2
  • 37
    • 48249138078 scopus 로고    scopus 로고
    • Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding
    • Zarrine-Afsar A, Wallin S, Neculai AM, Neudecker P, Howell PL, et al. (2008) Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding. Proc Natl Acad Sci USA 105: 9999-10004.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 9999-10004
    • Zarrine-Afsar, A.1    Wallin, S.2    Neculai, A.M.3    Neudecker, P.4    Howell, P.L.5
  • 38
    • 61549141060 scopus 로고    scopus 로고
    • Native topology of the designed protein Top7 is not conducive to cooperative folding
    • Zhang ZQ, Chan HS (2009) Native topology of the designed protein Top7 is not conducive to cooperative folding. Biophys J 96: L25-L27.
    • (2009) Biophys J , vol.96
    • Zhang, Z.Q.1    Chan, H.S.2
  • 39
    • 77649264931 scopus 로고    scopus 로고
    • Competition between native topology and nonnative interactions in simple and complex folding kinetics of natural and designed proteins
    • Zhang ZQ, Chan HS (2010) Competition between native topology and nonnative interactions in simple and complex folding kinetics of natural and designed proteins. Proc Natl Acad Sci USA 107: 2920-2925.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 2920-2925
    • Zhang, Z.Q.1    Chan, H.S.2
  • 41
    • 70349422120 scopus 로고    scopus 로고
    • Nonnative electrostatic interactions can modulate protein folding: Molecular dynamics with a grain of salt
    • Azia A, Levy Y (2009) Nonnative electrostatic interactions can modulate protein folding: molecular dynamics with a grain of salt. J Mol Biol 393: 527-542.
    • (2009) J Mol Biol , vol.393 , pp. 527-542
    • Azia, A.1    Levy, Y.2
  • 42
    • 36449000646 scopus 로고
    • Transition states and folding dynamics of proteins and heteropolymers
    • Chan HS, Dill KA (1994) Transition states and folding dynamics of proteins and heteropolymers. J Chem Phys 100: 9238-9257.
    • (1994) J Chem Phys , vol.100 , pp. 9238-9257
    • Chan, H.S.1    Dill, K.A.2
  • 43
    • 0242383943 scopus 로고    scopus 로고
    • Improved Gōlike models demonstrate the robustness of protein folding mechanisms towards non-native interactions
    • Karanicolas J, Brooks CL, III (2003) Improved Gōlike models demonstrate the robustness of protein folding mechanisms towards non-native interactions. J Mol Biol 334: 309-325.
    • (2003) J Mol Biol , vol.334 , pp. 309-325
    • Karanicolas, J.1    Brooks III, C.L.2
  • 44
    • 67749130905 scopus 로고    scopus 로고
    • The limited role of nonnative contacts in the folding pathways of a lattice protein
    • Gin BC, Garrahan JP, Geissler PL (2009) The limited role of nonnative contacts in the folding pathways of a lattice protein. J Mol Biol 392: 1303-1314.
    • (2009) J Mol Biol , vol.392 , pp. 1303-1314
    • Gin, B.C.1    Garrahan, J.P.2    Geissler, P.L.3
  • 45
    • 77954552237 scopus 로고    scopus 로고
    • Intermediate structure and slow hydration water dynamics in protein folding process
    • Gao M, Yao XQ, She ZS, Liu ZR, Zhu HQ (2010) Intermediate structure and slow hydration water dynamics in protein folding process. Acta Phys -Chim Sin 26: 1998-2006.
    • (2010) Acta Phys -Chim Sin , vol.26 , pp. 1998-2006
    • Gao, M.1    Yao, X.Q.2    She, Z.S.3    Liu, Z.R.4    Zhu, H.Q.5
  • 46
    • 0345306764 scopus 로고    scopus 로고
    • Design of a novel globular protein fold with atomic-level accuracy
    • Kuhlman B, Dantas G, Ireton GC, Varani G, Stoddard BL, et al. (2003) Design of a novel globular protein fold with atomic-level accuracy. Science 302: 1364-1368.
    • (2003) Science , vol.302 , pp. 1364-1368
    • Kuhlman, B.1    Dantas, G.2    Ireton, G.C.3    Varani, G.4    Stoddard, B.L.5
  • 47
    • 19744381543 scopus 로고    scopus 로고
    • Enhancement of association rates by nonspecific binding to DNA and cell membranes
    • Zhou H-X, Szabo A (2004) Enhancement of association rates by nonspecific binding to DNA and cell membranes. Phys Rev Lett 93: 178101.
    • (2004) Phys Rev Lett , vol.93 , pp. 178101
    • Zhou, H.-X.1    Szabo, A.2
  • 48
    • 25844493057 scopus 로고    scopus 로고
    • Change of the unbinding mechanism upon a mutation: A molecular dynamics study of an antibody-hapten complex
    • Curcio R, Caflisch A, Paci E (2005) Change of the unbinding mechanism upon a mutation: a molecular dynamics study of an antibody-hapten complex. Protein Sci 14: 2499-2514.
    • (2005) Protein Sci , vol.14 , pp. 2499-2514
    • Curcio, R.1    Caflisch, A.2    Paci, E.3
  • 49
    • 33746607765 scopus 로고    scopus 로고
    • Single-molecule dynamics reveals cooperative binding-folding in protein recognition
    • Wang J, Lu Q, Lu HP (2006) Single-molecule dynamics reveals cooperative binding-folding in protein recognition. PLoS Comput Biol 2: e78.
    • (2006) PLoS Comput Biol , vol.2
    • Wang, J.1    Lu, Q.2    Lu, H.P.3
  • 50
    • 40549134985 scopus 로고    scopus 로고
    • Electrostatic rate enhancement and transient complex of protein-protein association
    • Alsallaq R, Zhou H-X (2008) Electrostatic rate enhancement and transient complex of protein-protein association. Proteins 71: 320-335.
    • (2008) Proteins , vol.71 , pp. 320-335
    • Alsallaq, R.1    Zhou, H.-X.2
  • 51
    • 58149345492 scopus 로고    scopus 로고
    • Protein sliding along DNA: Dynamics and structural characterization
    • Givaty O, Levy Y (2009) Protein sliding along DNA: dynamics and structural characterization. J Mol Biol 385: 1087-1097.
    • (2009) J Mol Biol , vol.385 , pp. 1087-1097
    • Givaty, O.1    Levy, Y.2
  • 52
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright PE, Dyson HJ (1999) Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J Mol Biol 293: 321-331.
    • (1999) J Mol Biol , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 53
  • 54
    • 77954217602 scopus 로고    scopus 로고
    • The protein kingdom extended: Ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation
    • doi:10.1016/j.pbiomolbio.2010.01.003
    • Turoverov KK, Kuznetsova IM, Uversky VN (2010) The protein kingdom extended: ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregation. Prog Biophys Mol Biol; doi:10.1016/j.pbiomolbio.2010.01.003.
    • (2010) Prog Biophys Mol Biol
    • Turoverov, K.K.1    Kuznetsova, I.M.2    Uversky, V.N.3
  • 55
    • 77955046467 scopus 로고    scopus 로고
    • Intrinsically disordered proteins: The new sequencestructure- function relations
    • Huang YQ, Liu ZR (2010) Intrinsically disordered proteins: the new sequencestructure- function relations. Acta Phys -Chim Sin 26: 2061-2072.
    • (2010) Acta Phys -Chim Sin , vol.26 , pp. 2061-2072
    • Huang, Y.Q.1    Liu, Z.R.2
  • 56
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337: 635-645.
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 59
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson HJ, Wright PE (2002) Coupling of folding and binding for unstructured proteins. Curr Opin Struct Biol 12: 54-60.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 60
  • 61
    • 33947586778 scopus 로고    scopus 로고
    • Exploring the mechanism of flexible biomolecular recognition with single molecule dynamics
    • Lu Q, Lu HP, Wang J (2007) Exploring the mechanism of flexible biomolecular recognition with single molecule dynamics. Phys Rev Lett 98: 128105.
    • (2007) Phys Rev Lett , vol.98 , pp. 128105
    • Lu, Q.1    Lu, H.P.2    Wang, J.3
  • 62
    • 70350012289 scopus 로고    scopus 로고
    • Kinetic advantage of intrinsically disordered proteins in coupled folding-binding process: A critical assessment of the "fly-casting" mechanism
    • Huang YQ, Liu ZR (2009) Kinetic advantage of intrinsically disordered proteins in coupled folding-binding process: a critical assessment of the "fly-casting" mechanism. J Mol Biol 393: 1143-1159.
    • (2009) J Mol Biol , vol.393 , pp. 1143-1159
    • Huang, Y.Q.1    Liu, Z.R.2
  • 63
    • 78349244006 scopus 로고    scopus 로고
    • Smoothing molecular interactions: The "kinetic buffer" effect of intrinsically disordered proteins
    • DOI: 10.1002/ prot.22820
    • Huang YQ, Liu ZR (2010) Smoothing molecular interactions: the "kinetic buffer" effect of intrinsically disordered proteins. Proteins;DOI: 10.1002/ prot.22820.
    • (2010) Proteins;
    • Huang, Y.Q.1    Liu, Z.R.2
  • 64
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: The fly-casting mechanism
    • Shoemaker BA, Portman JJ, Wolynes PG (2000) Speeding molecular recognition by using the folding funnel: the fly-casting mechanism. Proc Natl Acad Sci USA 97: 8868-8873.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 65
    • 0027433708 scopus 로고
    • Phosphorylated CREB binds specifically to the nuclear protein CBP
    • Chrivia JC, Kwok RPS, Lamb N, Hagiwara M, Montminy MR, et al. (1993) Phosphorylated CREB binds specifically to the nuclear protein CBP. Nature 365: 855-859.
    • (1993) Nature , vol.365 , pp. 855-859
    • Chrivia, J.C.1    Kwok, R.P.S.2    Lamb, N.3    Hagiwara, M.4    Montminy, M.R.5
  • 66
    • 0344936739 scopus 로고    scopus 로고
    • Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: A model for activator:Coactivator interactions
    • Radhakrishnan I, Pérez-Alvarado GC, Parker D, Dyson HJ, Montminy MR, et al. (1997) Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions. Cell 91: 741-752.
    • (1997) Cell , vol.91 , pp. 741-752
    • Radhakrishnan, I.1    Pérez-Alvarado, G.C.2    Parker, D.3    Dyson, H.J.4    Montminy, M.R.5
  • 67
    • 33846625611 scopus 로고    scopus 로고
    • Fly-casting in protein-DNA binding: Frustration between protein folding and electrostatics facilitates target recognition
    • Levy Y, Onuchic JN, Wolynes PG (2007) Fly-casting in protein-DNA binding: frustration between protein folding and electrostatics facilitates target recognition. J Am Chem Soc 129: 738-739.
    • (2007) J Am Chem Soc , vol.129 , pp. 738-739
    • Levy, Y.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 68
    • 0029662315 scopus 로고    scopus 로고
    • Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: Conformational disorder mediates binding diversity
    • Kriwacki RW, Hengst L, Tennant L, Reed SI, Wright PE (1996) Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. Proc Natl Acad Sci USA 93: 11504-11509.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11504-11509
    • Kriwacki, R.W.1    Hengst, L.2    Tennant, L.3    Reed, S.I.4    Wright, P.E.5
  • 69
    • 40949117264 scopus 로고    scopus 로고
    • Flexible nets: Disorder and induced fit in the associations of p53 and 14-3-3 with their partners
    • Oldfield CJ, Meng JW, Yang JY, Yang MQ, Uversky VN, et al. (2008) Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners. Bmc Genomics 9: S1.
    • (2008) Bmc Genomics , vol.9
    • Oldfield, C.J.1    Meng, J.W.2    Yang, J.Y.3    Yang, M.Q.4    Uversky, V.N.5
  • 70
    • 67649852558 scopus 로고    scopus 로고
    • Physicochemical principles that regulate the competition between functional and dysfunctional association of proteins
    • Pechmann S, Levy ED, Tartaglia GG, Vendruscolo M (2009) Physicochemical principles that regulate the competition between functional and dysfunctional association of proteins. Proc Natl Acad Sci USA 106: 10159-10164.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 10159-10164
    • Pechmann, S.1    Levy, E.D.2    Tartaglia, G.G.3    Vendruscolo, M.4
  • 71
    • 34547943482 scopus 로고    scopus 로고
    • Molecular principles of the interactions of disordered proteins
    • Mészáros B, Tompa P, Simon I, Dosztányi Z (2007) Molecular principles of the interactions of disordered proteins. J Mol Biol 372: 549-561.
    • (2007) J Mol Biol , vol.372 , pp. 549-561
    • Mészáros, B.1    Tompa, P.2    Simon, I.3    Dosztányi, Z.4
  • 72
    • 67649635978 scopus 로고    scopus 로고
    • Intrinsic protein disorder and interaction promiscuity are widely associated with dosage sensitivity
    • Vavouri T, Semple JI, Garcia-Verdugo R, Lehner B (2009) Intrinsic protein disorder and interaction promiscuity are widely associated with dosage sensitivity. Cell 138: 198-208.
    • (2009) Cell , vol.138 , pp. 198-208
    • Vavouri, T.1    Semple, J.I.2    Garcia-Verdugo, R.3    Lehner, B.4
  • 73
    • 77649240855 scopus 로고    scopus 로고
    • Identifying the amylome, proteins capable of forming amyloid-like fibrils
    • Goldschmidt L, Teng PK, Riek R, Eisenberg D (2010) Identifying the amylome, proteins capable of forming amyloid-like fibrils. Proc Natl Acad Sci USA 107: 3487-3492.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 3487-3492
    • Goldschmidt, L.1    Teng, P.K.2    Riek, R.3    Eisenberg, D.4
  • 75
    • 27744500841 scopus 로고    scopus 로고
    • Solvation and desolvation effects in protein folding: Native flexibility, kinetic cooperativity and enthalpic barriers under isostability conditions
    • Liu ZR, Chan HS (2005) Solvation and desolvation effects in protein folding: native flexibility, kinetic cooperativity and enthalpic barriers under isostability conditions. Phys Biol 2: S75-S85.
    • (2005) Phys Biol , vol.2
    • Liu, Z.R.1    Chan, H.S.2
  • 76
    • 0037459035 scopus 로고    scopus 로고
    • Solvation effects and driving forces for protein thermodynamic and kinetic cooperativity: How adequate is native-centric topological modeling?
    • Kaya H, Chan HS (2003) Solvation effects and driving forces for protein thermodynamic and kinetic cooperativity: how adequate is native-centric topological modeling? J Mol Biol 326: 911-931.
    • (2003) J Mol Biol , vol.326 , pp. 911-931
    • Kaya, H.1    Chan, H.S.2
  • 77
    • 1642316280 scopus 로고    scopus 로고
    • Solvation effects and driving forces for protein thermodynamic and kinetic cooperativity: How adequate is native-centric topological modeling? Corrigendum
    • Kaya H, Chan HS (2004) Solvation effects and driving forces for protein thermodynamic and kinetic cooperativity: how adequate is native-centric topological modeling? Corrigendum. J Mol Biol 337: 1069-1070.
    • (2004) J Mol Biol , vol.337 , pp. 1069-1070
    • Kaya, H.1    Chan, H.S.2
  • 78
    • 0000764091 scopus 로고
    • Constant-temperature free energy surfaces for physical and chemical processes
    • Boczko EM, Brooks III CL (1993) Constant-temperature free energy surfaces for physical and chemical processes. J Phys Chem 97: 4509-4513.
    • (1993) J Phys Chem , vol.97 , pp. 4509-4513
    • Boczko, E.M.1    Brooks III, C.L.2
  • 79
    • 54949099933 scopus 로고    scopus 로고
    • Probing possible downhill folding: Native contact topology likely places a significant constraint on the folding cooperativity of proteins with,40 residues
    • Badasyan A, Liu ZR, Chan HS (2008) Probing possible downhill folding: native contact topology likely places a significant constraint on the folding cooperativity of proteins with,40 residues. J Mol Biol 384: 512-530.
    • (2008) J Mol Biol , vol.384 , pp. 512-530
    • Badasyan, A.1    Liu, Z.R.2    Chan, H.S.3


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