메뉴 건너뛰기




Volumn 8, Issue 6, 1999, Pages 1181-1190

Folding funnels, binding funnels, and protein function

Author keywords

Binding funnels; Conformational ensembles; Energy landscape; Folding funnels; Function; Misfolding

Indexed keywords

ENDONUCLEASE; PROTEIN;

EID: 0033056708     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.6.1181     Document Type: Review
Times cited : (589)

References (66)
  • 1
    • 0028286471 scopus 로고
    • Kinetics versus thermodynamics in protein folding
    • Baker D, Agard DA. 1994. Kinetics versus thermodynamics in protein folding. Biochemistry 33:7505-1509.
    • (1994) Biochemistry , vol.33 , pp. 7505-11509
    • Baker, D.1    Agard, D.A.2
  • 2
    • 0028776642 scopus 로고
    • Matching speed and stability
    • Baldwin RL. 1994. Matching speed and stability. Nature 369:183-184.
    • (1994) Nature , vol.369 , pp. 183-184
    • Baldwin, R.L.1
  • 3
    • 0029249945 scopus 로고
    • The nature of protein folding pathways: The classical versus the new view
    • Baldwin RL. 1995. The nature of protein folding pathways: The classical versus the new view. J Biomol NMR 5:103-109.
    • (1995) J Biomol NMR , vol.5 , pp. 103-109
    • Baldwin, R.L.1
  • 4
    • 0032972986 scopus 로고    scopus 로고
    • Is protein folding hierarchic? I. Local structure and peptide folding
    • Baldwin RL, Rose GD. 1999. Is protein folding hierarchic? I. Local structure and peptide folding. Trends Biochem Sci 24:26-33.
    • (1999) Trends Biochem Sci , vol.24 , pp. 26-33
    • Baldwin, R.L.1    Rose, G.D.2
  • 5
    • 0029973119 scopus 로고    scopus 로고
    • Direct observation of fast protein folding: The initial collapse of apomyoglobin
    • Ballew RM, Sabelko J, Gruebele M. 1996. Direct observation of fast protein folding: The initial collapse of apomyoglobin. Proc Natl Acad Sci USA 93:5759-5764.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5759-5764
    • Ballew, R.M.1    Sabelko, J.2    Gruebele, M.3
  • 7
    • 0000370391 scopus 로고    scopus 로고
    • The topology of multidimensional potential energy surfaces: Theory and application to peptide structure and kinetics
    • Becker OM, Karplus M. 1997. The topology of multidimensional potential energy surfaces: Theory and application to peptide structure and kinetics. J Chem Phys 106:1495-1517.
    • (1997) J Chem Phys , vol.106 , pp. 1495-1517
    • Becker, O.M.1    Karplus, M.2
  • 8
    • 0028204771 scopus 로고
    • Domain swapping: Entangling alliances between proteins
    • Bennett MJ, Choe S, Eisenberg D. 1994. Domain swapping: Entangling alliances between proteins. Proc Natl Acad Sci USA 91:3127-3131.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3127-3131
    • Bennett, M.J.1    Choe, S.2    Eisenberg, D.3
  • 9
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • Bennett MJ, Schlunegger MP, Eisenberg D. 1995. 3D domain swapping: A mechanism for oligomer assembly. Protein Sci 4:2455-2468.
    • (1995) Protein Sci , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 10
    • 0024733407 scopus 로고
    • Intermediates and barrier crossing in a random energy model (with applications to protein folding)
    • Bryngelson JD, Wolynes PG. 1989. Intermediates and barrier crossing in a random energy model (with applications to protein folding). J Phys Chem 93:6902-6915.
    • (1989) J Phys Chem , vol.93 , pp. 6902-6915
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 11
    • 0031430923 scopus 로고    scopus 로고
    • Recognition between disordered states: Kinetics of the self-assembly of thioredoxin fragments
    • Chaffotte AF, Li JH, Georgescu RE, Goldberg ME, Tasayco ML. 1997. Recognition between disordered states: Kinetics of the self-assembly of thioredoxin fragments. Biochemistry 36:16040-16048.
    • (1997) Biochemistry , vol.36 , pp. 16040-16048
    • Chaffotte, A.F.1    Li, J.H.2    Georgescu, R.E.3    Goldberg, M.E.4    Tasayco, M.L.5
  • 12
    • 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
  • 13
    • 0003166498 scopus 로고    scopus 로고
    • Protein folding in the landscape perspective: Chevron plots and non-Arrhenius kinetics
    • Chan HS, Dill KA. 1998. Protein folding in the landscape perspective: Chevron plots and non-Arrhenius kinetics. Proteins 30:2-33.
    • (1998) Proteins , vol.30 , pp. 2-33
    • Chan, H.S.1    Dill, K.A.2
  • 14
    • 0027530108 scopus 로고
    • Protein docking algorithms: Simulating molecular recognition
    • Cherfils J, Janin J. 1993. Protein docking algorithms: Simulating molecular recognition. Curr Opin Struct Biol 3:265-269.
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 265-269
    • Cherfils, J.1    Janin, J.2
  • 16
    • 0029190841 scopus 로고
    • Oligomer evolution in action
    • D'Alessio G. 1995. Oligomer evolution in action. Nat Struct Biol 2:11-13.
    • (1995) Nat Struct Biol , vol.2 , pp. 11-13
    • D'Alessio, G.1
  • 17
    • 0032993447 scopus 로고    scopus 로고
    • Polymer principles and protein folding
    • Dill KA. 1999. Polymer principles and protein folding. Protein Sci 8:1166-1180.
    • (1999) Protein Sci , vol.8 , pp. 1166-1180
    • Dill, K.A.1
  • 18
    • 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
  • 19
    • 0030788883 scopus 로고    scopus 로고
    • Protein structure and energy landscape dependence on sequence using a continuous energy function
    • Dill KA, Phillips, AT, Rosen JB. 1997. Protein structure and energy landscape dependence on sequence using a continuous energy function. J Comp Biol 4:227-239.
    • (1997) J Comp Biol , vol.4 , pp. 227-239
    • Dill, K.A.1    Phillips, A.T.2    Rosen, J.B.3
  • 20
    • 0030627637 scopus 로고    scopus 로고
    • Meeting review: The second meeting on the critical assessment of techniques for protein structure prediction (CASP2), Asilomar, California, December 13-16, 1996
    • Dunbrack RL, Gerloff DL, Bower M, Chen X, Lichtarge O, Cohen FE. 1997. Meeting review: The second meeting on the critical assessment of techniques for protein structure prediction (CASP2), Asilomar, California, December 13-16, 1996. Folding Design 2:R27-R42.
    • (1997) Folding Design , vol.2
    • Dunbrack, R.L.1    Gerloff, D.L.2    Bower, M.3    Chen, X.4    Lichtarge, O.5    Cohen, F.E.6
  • 22
    • 0031043161 scopus 로고    scopus 로고
    • Nucleation mechanisms in protein folding
    • Fersht AR. 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
  • 23
    • 0029025913 scopus 로고
    • A geometry-based suite of molecular docking processes
    • Fischer D, Lin SL, Wolfson HJ, Nussinov, R. 1995. A geometry-based suite of molecular docking processes. J Mol Biol 248:459-411.
    • (1995) J Mol Biol , vol.248 , pp. 459-1411
    • Fischer, D.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 25
    • 0027943261 scopus 로고
    • Conformational isomerism and the diversity of antibodies
    • Foote J, Milstein C. 1994. Conformational isomerism and the diversity of antibodies. Proc Natl Acad Sci USA 91:10370-10374.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10370-10374
    • Foote, J.1    Milstein, C.2
  • 26
    • 0031708076 scopus 로고    scopus 로고
    • The energy landscape in non-biological molecules
    • Frauenfelder H, Leeson DT. 1998. The energy landscape in non-biological molecules. Nat Struct Biol 5:757-759.
    • (1998) Nat Struct Biol , vol.5 , pp. 757-759
    • Frauenfelder, H.1    Leeson, D.T.2
  • 27
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder H, Sligar SG, Wolynes PG. 1991. The energy landscapes and motions of proteins. Science 254:1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 28
    • 0031856887 scopus 로고    scopus 로고
    • Satisfying turns in folding transitions
    • Gruebele M, Wolynes P. 1998. Satisfying turns in folding transitions. Nat Struct Biol 5:662-665.
    • (1998) Nat Struct Biol , vol.5 , pp. 662-665
    • Gruebele, M.1    Wolynes, P.2
  • 29
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett JT, Lansbury PT Jr. 1993. Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73:1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury P.T., Jr.2
  • 30
    • 0030626588 scopus 로고    scopus 로고
    • The Levinthal paradox: Yesterday and today
    • Karplus M. 1997. The Levinthal paradox: yesterday and today. Folding Design 2:S69-S75.
    • (1997) Folding Design , vol.2
    • Karplus, M.1
  • 31
    • 85069123887 scopus 로고
    • Comment: Kinetics of protein folding
    • Karplus M, Sali A, Shakhnovitch E. 1995. Comment: Kinetics of protein folding. Nature 373:664-665.
    • (1995) Nature , vol.373 , pp. 664-665
    • Karplus, M.1    Sali, A.2    Shakhnovitch, E.3
  • 32
    • 0002770218 scopus 로고
    • Protein folding: Theoretical studies of thermodynamics and dynamics
    • Creighton T, ed. New York: WH Freeman & Sons
    • Karplus M, Shakhnovitch E. 1992. Protein folding: Theoretical studies of thermodynamics and dynamics. In: Creighton T, ed. Protein folding. New York: WH Freeman & Sons, pp 127-195.
    • (1992) Protein Folding , pp. 127-195
    • Karplus, M.1    Shakhnovitch, E.2
  • 33
    • 0026572775 scopus 로고
    • Molecular surface recognition: Determination of geometric fit between protein and their ligands by correlation techniques
    • Katchalski-Katzir E, Shariv I, Eisenstein M, Friesem AA, Aflalo C, Vakser IA. 1992. Molecular surface recognition: Determination of geometric fit between protein and their ligands by correlation techniques. Proc Natl Acad Sci USA 89:2195-2199.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 2195-2199
    • Katchalski-Katzir, E.1    Shariv, I.2    Eisenstein, M.3    Friesem, A.A.4    Aflalo, C.5    Vakser, I.A.6
  • 34
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland DE Jr. 1958. Application of a theory of enzyme specificity to protein synthesis. Proc Natl Acad Sci USA 44:98-123.
    • (1958) Proc Natl Acad Sci USA , vol.44 , pp. 98-123
    • Koshland D.E., Jr.1
  • 35
    • 0031576341 scopus 로고    scopus 로고
    • Complementation of peptide fragments of the single domain protein chymotrypsin inhibitor 2
    • Ladurner AG, Itzhaki LS, Gay FDP, Fersht AR. 1997. Complementation of peptide fragments of the single domain protein chymotrypsin inhibitor 2. J Mol Biol 273:317-329.
    • (1997) J Mol Biol , vol.273 , pp. 317-329
    • Ladurner, A.G.1    Itzhaki, L.S.2    Gay, F.D.P.3    Fersht, A.R.4
  • 36
    • 0031465967 scopus 로고    scopus 로고
    • "New view" of protein folding reconciled with the old through multiple unfolding simulations
    • Lazaridis T, Karplus M. 1997. "New view" of protein folding reconciled with the old through multiple unfolding simulations. Science 274:1928-1931.
    • (1997) Science , vol.274 , pp. 1928-1931
    • Lazaridis, T.1    Karplus, M.2
  • 37
    • 0031670902 scopus 로고    scopus 로고
    • Conformational switching in an aspartic proteinase
    • Lee AY, Gulnik SV, Erickson JW. 1998. Conformational switching in an aspartic proteinase. Nat Struct Biol 5:866-871.
    • (1998) Nat Struct Biol , vol.5 , pp. 866-871
    • Lee, A.Y.1    Gulnik, S.V.2    Erickson, J.W.3
  • 39
    • 0031825181 scopus 로고    scopus 로고
    • Obligatory steps in protein folding and the conformational diversity of the transition state
    • Martinez JC, Pisabarro MT, Serrano L. 1998. Obligatory steps in protein folding and the conformational diversity of the transition state. Nat Struct Biol 5:721-729.
    • (1998) Nat Struct Biol , vol.5 , pp. 721-729
    • Martinez, J.C.1    Pisabarro, M.T.2    Serrano, L.3
  • 40
    • 0030867610 scopus 로고    scopus 로고
    • Ligand binding to proteins: The binding landscape model
    • Miller DW, Dill KA. 1997. Ligand binding to proteins: The binding landscape model. Protein Sci 6:2166-2179.
    • (1997) Protein Sci , vol.6 , pp. 2166-2179
    • Miller, D.W.1    Dill, K.A.2
  • 41
    • 0031837984 scopus 로고    scopus 로고
    • Hinge bending within the cytokine receptor superfamily revealed by the 2.4 å crystal structure of the extracellular domain of the rabbit tissue factor
    • Muller Y, Kelley RF, De Vos AM. 1998. Hinge bending within the cytokine receptor superfamily revealed by the 2.4 Å crystal structure of the extracellular domain of the rabbit tissue factor. Protein Sci 7:1106-1115.
    • (1998) Protein Sci , vol.7 , pp. 1106-1115
    • Muller, Y.1    Kelley, R.F.2    De Vos, A.M.3
  • 42
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • Netzer WJ, Hartl FU. 1997. Recombination of protein domains facilitated by co-translational folding in eukaryotes. Nature 388:343-349.
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.J.1    Hartl, F.U.2
  • 43
    • 0028166881 scopus 로고
    • Shape complementarity at protein-protein interfaces
    • Norel R, Lin SL, Wolfson H, Nussinov R. 1994. Shape complementarity at protein-protein interfaces. Biopolymers 34:933-940.
    • (1994) Biopolymers , vol.34 , pp. 933-940
    • Norel, R.1    Lin, S.L.2    Wolfson, H.3    Nussinov, R.4
  • 44
    • 0029089732 scopus 로고
    • Molecular surface complementarity at protein-protein interfaces: The critical role played by surface normals at well placed, sparse, points in docking
    • Norel R, Lin SL, Wolfson H, Nussinov R. 1995. Molecular surface complementarity at protein-protein interfaces: The critical role played by surface normals at well placed, sparse, points in docking. J Mol Biol 252:263-273.
    • (1995) J Mol Biol , vol.252 , pp. 263-273
    • Norel, R.1    Lin, S.L.2    Wolfson, H.3    Nussinov, R.4
  • 45
    • 0026607545 scopus 로고
    • Kinetics of protein-protein association explained by Brownian dynamics computer simulation
    • Northrup SH, Erickson HP. 1992. Kinetics of protein-protein association explained by Brownian dynamics computer simulation. Proc Natl Acad Sci USA 89:3338-3342.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 3338-3342
    • Northrup, S.H.1    Erickson, H.P.2
  • 47
    • 0028914722 scopus 로고
    • Structural basis of substrate specificity in the serine proteases
    • Perona JJ, Craik CS. 1995. Structural basis of substrate specificity in the serine proteases. Protein Sci 4:337-360.
    • (1995) Protein Sci , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 49
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner SB. 1991. Molecular biology of prion diseases. Science 252:1515-1522.
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 50
    • 0029027777 scopus 로고
    • NMR study of the reconstitution of the β-sheet of thioredoxin by fragment complementation
    • Tasayco ML, Chao K. 1995. NMR study of the reconstitution of the β-sheet of thioredoxin by fragment complementation. Proteins SFG 22:41-44.
    • (1995) Proteins SFG , vol.22 , pp. 41-44
    • Tasayco, M.L.1    Chao, K.2
  • 51
    • 0029988383 scopus 로고    scopus 로고
    • Protein-protein interfaces: Architectures and interactions in protein-protein interfaces and in protein cores. Their similarities and differences
    • Tsai CJ, Lin SL, Wolfson, H, Nussinov R. 1996. Protein-protein interfaces: Architectures and interactions in protein-protein interfaces and in protein cores. Their similarities and differences. Critic Rev Biochem Mol Biol 31:127-152.
    • (1996) Critic Rev Biochem Mol Biol , vol.31 , pp. 127-152
    • Tsai, C.J.1    Lin, S.L.2    Wolfson, H.3    Nussinov, R.4
  • 52
    • 1842405464 scopus 로고    scopus 로고
    • Studies of protein-protein interfaces: Statistical analysis of the hydrophobic effect
    • Tsai CJ, Lin SL, Wolfson, H, Nussinov R. 1997a. Studies of protein-protein interfaces: Statistical analysis of the hydrophobic effect. Protein Sci 6:53-64.
    • (1997) Protein Sci , vol.6 , pp. 53-64
    • Tsai, C.J.1    Lin, S.L.2    Wolfson, H.3    Nussinov, R.4
  • 53
    • 0032777204 scopus 로고    scopus 로고
    • Distinguishing between sequential and non-sequentially folded protein: Implications for folding and misfolding
    • In press
    • Tsai CJ, Maizel JV Jr, Nussinov R. 1999. Distinguishing between sequential and non-sequentially folded protein: Implications for folding and misfolding. Protein Sci. In press.
    • (1999) Protein Sci.
    • Tsai, C.J.1    Maizel J.V., Jr.2    Nussinov, R.3
  • 54
    • 0031012563 scopus 로고    scopus 로고
    • Hydrophobic folding units derived from dissimilar monomer structures and their interactions
    • Tsai CJ, Nussinov R. 1997. Hydrophobic folding units derived from dissimilar monomer structures and their interactions. Protein Sci 6:24-42.
    • (1997) Protein Sci , vol.6 , pp. 24-42
    • Tsai, C.J.1    Nussinov, R.2
  • 55
    • 0030768266 scopus 로고    scopus 로고
    • Structural motifs at protein-protein interfaces: Protein cores versus two-state and three-state model complexes
    • Tsai CJ, Xu D, Nussinov R. 1997b. Structural motifs at protein-protein interfaces: Protein cores versus two-state and three-state model complexes. Protein Sci 6:1793-1805.
    • (1997) Protein Sci , vol.6 , pp. 1793-1805
    • Tsai, C.J.1    Xu, D.2    Nussinov, R.3
  • 56
    • 0031868211 scopus 로고    scopus 로고
    • Protein folding via binding, and vice versa
    • Tsai CJ, Xu D, Nussinov R. 1998. Protein folding via binding, and vice versa. Folding Design 3:R71-R80.
    • (1998) Folding Design , vol.3
    • Tsai, C.J.1    Xu, D.2    Nussinov, R.3
  • 57
    • 0030055657 scopus 로고    scopus 로고
    • Exploring the energy landscapes of molecular recognition by a genetic algorithm: Analysis of the requirements for robust docking of HIV-1 protease and FKBP-12 complexes
    • Verkhivker GM, Rejto PA, Gehlhaar DK, Freer ST. 1996. Exploring the energy landscapes of molecular recognition by a genetic algorithm: Analysis of the requirements for robust docking of HIV-1 protease and FKBP-12 complexes. Proteins SFG 250:342-352.
    • (1996) Proteins SFG , vol.250 , pp. 342-352
    • Verkhivker, G.M.1    Rejto, P.A.2    Gehlhaar, D.K.3    Freer, S.T.4
  • 58
  • 59
    • 0029786948 scopus 로고    scopus 로고
    • A dynamic bundle of four adjacent hydrophobic segments in the denatured state of staphylococcal nuclease
    • Wang Y, Shortle D. 1996. A dynamic bundle of four adjacent hydrophobic segments in the denatured state of staphylococcal nuclease. Protein Sci 5:1898-1906.
    • (1996) Protein Sci , vol.5 , pp. 1898-1906
    • Wang, Y.1    Shortle, D.2
  • 61
    • 0030050701 scopus 로고    scopus 로고
    • Binding in the growth hormone receptor complex
    • Wells JA. 1996. Binding in the growth hormone receptor complex. Proc Natl Acad Sci USA 93:1-6.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1-6
    • Wells, J.A.1
  • 63
    • 0028950075 scopus 로고
    • Forces of tertiary structural organization in globular proteins
    • Yue K, Dill KA. 1995. Forces of tertiary structural organization in globular proteins. Proc Natl Acad Sci USA 92:146-150.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 146-150
    • Yue, K.1    Dill, K.A.2
  • 64
    • 0031561809 scopus 로고    scopus 로고
    • Protein binding versus protein folding: The role of hydrophilic bridges in protein association
    • Xu D, Lin SL, Nussinov R. 1997. Protein binding versus protein folding: The role of hydrophilic bridges in protein association. J Mol Biol 265:68-84.
    • (1997) J Mol Biol , vol.265 , pp. 68-84
    • Xu, D.1    Lin, S.L.2    Nussinov, R.3
  • 65
    • 0031913197 scopus 로고    scopus 로고
    • Mechanism and evolution of protein dimerization
    • Xu D, Tsai CJ, Nussinov R. 1998. Mechanism and evolution of protein dimerization. Protein Sci 7:533-544.
    • (1998) Protein Sci , vol.7 , pp. 533-544
    • Xu, D.1    Tsai, C.J.2    Nussinov, R.3
  • 66
    • 0033081069 scopus 로고    scopus 로고
    • Protein-protein recognition: Exploring the energy funnels near the binding sites
    • Zhang C, Chen J, DeLisi C. 1999. Protein-protein recognition: Exploring the energy funnels near the binding sites. Proteins SFG 34:255-267.
    • (1999) Proteins SFG , vol.34 , pp. 255-267
    • Zhang, C.1    Chen, J.2    Delisi, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.