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Volumn 6, Issue 7, 1997, Pages 1426-1437

Hydrophobic folding units at protein-protein interfaces: Implications to protein folding and to protein-protein association

Author keywords

Compactness; Folding unit; Hydrophobic core; Protein binding; Protein folding; Protein protein association

Indexed keywords

CALBINDIN; CYSTATIN; MONELLIN; TROPONIN C;

EID: 0030756203     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060707     Document Type: Article
Times cited : (115)

References (48)
  • 1
    • 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
  • 3
    • 0018270134 scopus 로고
    • The three structural organization of proteins
    • Crippen GM. 1978. The three structural organization of proteins. J Mol Biol 126:315-332.
    • (1978) J Mol Biol , vol.126 , pp. 315-332
    • Crippen, G.M.1
  • 4
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA. 1990. Dominant forces in protein folding. Biochemistry 31:7134-7155.
    • (1990) Biochemistry , vol.31 , pp. 7134-7155
    • Dill, K.A.1
  • 5
  • 6
    • 0028958601 scopus 로고
    • Characterizing transition states in protein folding: An essential step in the puzzle
    • Fersht AR. 1994a. Characterizing transition states in protein folding: An essential step in the puzzle. Curr Opin Str Biol 5:79-84.
    • (1994) Curr Opin Str Biol , vol.5 , pp. 79-84
    • Fersht, A.R.1
  • 7
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
    • Fersht AR. 1994b. Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications. Proc Natl Acad Sci 92:10869-10873.
    • (1994) Proc Natl Acad Sci , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 8
    • 0028230909 scopus 로고
    • 3-D, sequence-order independent structural comparison of trypsin against the crystallographic database reveals active site similarities to subtilisin-like and sulfhydryl proteases: Potential implications
    • Fischer D, Wolfson H, Lin SL, Nussinov R. 1994. 3-D, sequence-order independent structural comparison of trypsin against the crystallographic database reveals active site similarities to subtilisin-like and sulfhydryl proteases: Potential implications. Protein Sci 5:769-786.
    • (1994) Protein Sci , vol.5 , pp. 769-786
    • Fischer, D.1    Wolfson, H.2    Lin, S.L.3    Nussinov, R.4
  • 9
    • 0001848681 scopus 로고
    • Folding of large proteins:multidomain and multisubunit proteins
    • Creighton TE, ed. New York: W. H. Freeman and Company
    • Garel JR. 1992. Folding of large proteins:multidomain and multisubunit proteins. In: Creighton TE, ed. Protein folding. New York: W. H. Freeman and Company, pp 405-454.
    • (1992) Protein Folding , pp. 405-454
    • Garel, J.R.1
  • 10
    • 0025334690 scopus 로고
    • Folding and stability of trp aporepressor from Escherichia coli
    • Gittelman MS, Matthews CR. 1990. Folding and stability of trp aporepressor from Escherichia coli. Biochemistry 29:7011-7020.
    • (1990) Biochemistry , vol.29 , pp. 7011-7020
    • Gittelman, M.S.1    Matthews, C.R.2
  • 12
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • Hendsch BZS, Tidor B. 1994. Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci 3:211-226.
    • (1994) Protein Sci , vol.3 , pp. 211-226
    • Hendsch, B.Z.S.1    Tidor, B.2
  • 13
    • 0000678373 scopus 로고
    • Reciprocal averaging: An eigenvector method of ordination
    • Hill MO. 1973. Reciprocal averaging: An eigenvector method of ordination. J Ecol 67:237-251.
    • (1973) J Ecol , vol.67 , pp. 237-251
    • Hill, M.O.1
  • 14
    • 0028290005 scopus 로고
    • Parser for protein folding units
    • Holm L, Sander C. 1994. Parser for protein folding units. Proteins 19:256-268.
    • (1994) Proteins , vol.19 , pp. 256-268
    • Holm, L.1    Sander, C.2
  • 15
    • 0001842441 scopus 로고    scopus 로고
    • Adding backbone to protein folding: Why proteins are polypeptides
    • Honig B, Cohen FE. 1996. Adding backbone to protein folding: Why proteins are polypeptides. Folding & Design 1:R17-R20.
    • (1996) Folding & Design , vol.1
    • Honig, B.1    Cohen, F.E.2
  • 16
    • 0028891784 scopus 로고
    • Identification and analysis of domains in proteins
    • Islam SA, Luo J, Sternberg MJ. 1995. Identification and analysis of domains in proteins. Protein Eng 5:513-525.
    • (1995) Protein Eng , vol.5 , pp. 513-525
    • Islam, S.A.1    Luo, J.2    Sternberg, M.J.3
  • 17
    • 0027282636 scopus 로고
    • Genetic fusion of subunits of a dimeric protein substantially enhances its stability and rate of folding
    • Liang H, Sandberg WS, Terwillinger TC. 1993. Genetic fusion of subunits of a dimeric protein substantially enhances its stability and rate of folding. Proc Natl Acad Sci 90:7010-7014.
    • (1993) Proc Natl Acad Sci , vol.90 , pp. 7010-7014
    • Liang, H.1    Sandberg, W.S.2    Terwillinger, T.C.3
  • 18
    • 0019588920 scopus 로고
    • Folding units in globular proteins
    • Lesk AM, Rose GD. 1981. Folding units in globular proteins. Proc Natl Acad Sci 75:4304-4308.
    • (1981) Proc Natl Acad Sci , vol.75 , pp. 4304-4308
    • Lesk, A.M.1    Rose, G.D.2
  • 19
    • 0015222647 scopus 로고
    • The interpretation of protein structures. Estimation of static accessibility
    • Lee BK, Richards FM. 1971. The interpretation of protein structures. Estimation of static accessibility. J Mol Biol 55:379-400.
    • (1971) J Mol Biol , vol.55 , pp. 379-400
    • Lee, B.K.1    Richards, F.M.2
  • 20
    • 0028325298 scopus 로고
    • P22 Arc repressor. Folding kinetics of a single-domain, dimeric protein
    • Milla ME, Sauer RT. 1994. P22 Arc repressor. Folding kinetics of a single-domain, dimeric protein. Biochemistry 33:1125-1133.
    • (1994) Biochemistry , vol.33 , pp. 1125-1133
    • Milla, M.E.1    Sauer, R.T.2
  • 22
    • 0025906759 scopus 로고
    • An analysis of protein folding pathways
    • Moult J, Unger R. 1991. An analysis of protein folding pathways. Biochemistry 50:3816-3824.
    • (1991) Biochemistry , vol.50 , pp. 3816-3824
    • Moult, J.1    Unger, R.2
  • 23
    • 0026649261 scopus 로고
    • Molecular basis of cooperativity in protein folding. II. Structural identification of cooperative folding units and folding intermediates
    • Murphy K, Bhakuni V, Vie D, Freire E. 1992. Molecular basis of cooperativity in protein folding. II. Structural identification of cooperative folding units and folding intermediates. J Mol Biol 227:293-306.
    • (1992) J Mol Biol , vol.227 , pp. 293-306
    • Murphy, K.1    Bhakuni, V.2    Vie, D.3    Freire, E.4
  • 25
    • 0025719208 scopus 로고
    • Efficient detection of motifs in biological macromolecules by computer vision techniques
    • Nussinov R, Wolfson HJ. 1991. Efficient detection of motifs in biological macromolecules by computer vision techniques. Proc Natl Acad Sci 88:10495-10499.
    • (1991) Proc Natl Acad Sci , vol.88 , pp. 10495-10499
    • Nussinov, R.1    Wolfson, H.J.2
  • 26
    • 0002693020 scopus 로고
    • Physical basis of the stability of the folded conformations of proteins
    • Creighton TE, ed. New York: W. H. Freeman and Company
    • Privalov PL. 1992. Physical basis of the stability of the folded conformations of proteins. In: Creighton TE, ed. Protein folding. New York: W. H. Freeman and Company, pp 83-126.
    • (1992) Protein Folding , pp. 83-126
    • Privalov, P.L.1
  • 27
    • 0030010408 scopus 로고    scopus 로고
    • Intermediate states in protein folding
    • Privalov PL. 1996. Intermediate states in protein folding. J Mol Biol 255:707-725.
    • (1996) J Mol Biol , vol.255 , pp. 707-725
    • Privalov, P.L.1
  • 28
    • 0019874608 scopus 로고
    • Location of domains in globular proteins
    • Rashin AA. 1981. Location of domains in globular proteins. Nature 291:85-87.
    • (1981) Nature , vol.291 , pp. 85-87
    • Rashin, A.A.1
  • 29
    • 0023776967 scopus 로고
    • Identification of regions of potential flexibility in protein structures: Folding units and correlations with intron positions
    • Segawa S, Richards FM. 1988. Identification of regions of potential flexibility in protein structures: Folding units and correlations with intron positions. Biopolymers 27:23-40.
    • (1988) Biopolymers , vol.27 , pp. 23-40
    • Segawa, S.1    Richards, F.M.2
  • 30
    • 0029670994 scopus 로고    scopus 로고
    • Conserved residues and the mechanism of protein folding
    • Shakhnovitch E, Abkevich V, Ptitsyn O. 1996. Conserved residues and the mechanism of protein folding. Nature 379:96-98.
    • (1996) Nature , vol.379 , pp. 96-98
    • Shakhnovitch, E.1    Abkevich, V.2    Ptitsyn, O.3
  • 31
    • 0028943588 scopus 로고
    • Continuous and discontinuous domains: An algorithm for the automatic generation of reliable protein domain definitions
    • Siddiqui AS. Barton GJ. 1995. Continuous and discontinuous domains: An algorithm for the automatic generation of reliable protein domain definitions. Protein Sci 4:872-884.
    • (1995) Protein Sci , vol.4 , pp. 872-884
    • Siddiqui, A.S.1    Barton, G.J.2
  • 32
    • 0028914725 scopus 로고
    • An automatic method involving cluster analysis of secondary structures for the identification of domains in proteins
    • Sowdhamini R, Blundell TL. 1995. An automatic method involving cluster analysis of secondary structures for the identification of domains in proteins. Protein Sci 4:506-520.
    • (1995) Protein Sci , vol.4 , pp. 506-520
    • Sowdhamini, R.1    Blundell, T.L.2
  • 33
    • 0028937153 scopus 로고
    • A procedure for detecting structural domains in proteins
    • Swindell MB. 1995. A procedure for detecting structural domains in proteins. Protein Sci 4:103-112.
    • (1995) Protein Sci , vol.4 , pp. 103-112
    • Swindell, M.B.1
  • 34
    • 0026596758 scopus 로고
    • Ordered self-assembly of polypeptide fragments to form nativelike dimeric trp repressor
    • Tasayco ML, Carey J. 1992. Ordered self-assembly of polypeptide fragments to form nativelike dimeric trp repressor. Science 255:594-597.
    • (1992) Science , vol.255 , pp. 594-597
    • Tasayco, M.L.1    Carey, J.2
  • 35
    • 0029760325 scopus 로고    scopus 로고
    • Domain swapping creates a third putative combining site in bovine odorant binding protein dimer
    • Tegoni M, Ramoni R, Bignetti E, Spinelli S, Cambillau C. 1996. Domain swapping creates a third putative combining site in bovine odorant binding protein dimer. Nature Struct Biol 3:863-867.
    • (1996) Nature Struct Biol , vol.3 , pp. 863-867
    • Tegoni, M.1    Ramoni, R.2    Bignetti, E.3    Spinelli, S.4    Cambillau, C.5
  • 36
    • 0030602896 scopus 로고    scopus 로고
    • A dataset of protein-protein interfaces generated with a sequence-order-independent comparison technique
    • Tsai C-J, Lin SL, Wolfson HJ, Nussinov R. 1996. A dataset of protein-protein interfaces generated with a sequence-order-independent comparison technique. J Mol Biol 260:604-620.
    • (1996) J Mol Biol , vol.260 , pp. 604-620
    • Tsai, C.-J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 37
    • 1842405464 scopus 로고    scopus 로고
    • Studies of protein-protein interfaces: A statistical analysis of the hydrophobic effect
    • Tsai C-J, Lin SL, Wolfson HJ, Nussinov R. 1997a. Studies of protein-protein interfaces: A 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.J.3    Nussinov, R.4
  • 38
    • 0031012563 scopus 로고    scopus 로고
    • Hydrophobic folding units derived from dissimilar monomer structures and their interactions
    • Tsai C-J, 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
  • 39
    • 0030768266 scopus 로고    scopus 로고
    • Structural motifs at protein-protein interfaces: Protein cores versus two-state and three-state model complexes
    • in press
    • Tsai C-J, Xu D, Nussinov R. 1997b. Structural motifs at protein-protein interfaces: Protein cores versus two-state and three-state model complexes. Protein Sci, in press.
    • (1997) Protein Sci
    • Tsai, C.-J.1    Xu, D.2    Nussinov, R.3
  • 40
    • 0028932770 scopus 로고
    • The order of the secondary structure elements does not determine the structure of a protein but does affect its folding kinetics
    • Viguera AR, Blanco FJ, Serrano L. 1995. The order of the secondary structure elements does not determine the structure of a protein but does affect its folding kinetics. J Mol Biol 247:670-681.
    • (1995) J Mol Biol , vol.247 , pp. 670-681
    • Viguera, A.R.1    Blanco, F.J.2    Serrano, L.3
  • 41
    • 0019877668 scopus 로고
    • Location of structural domains in proteins
    • Wodak SJ, Janin J. 1981. Location of structural domains in proteins. Biochemistry 20:6544-6552.
    • (1981) Biochemistry , vol.20 , pp. 6544-6552
    • Wodak, S.J.1    Janin, J.2
  • 42
    • 0026464639 scopus 로고
    • New algorithm to model protein-protein recognition based on surface complementarity
    • Walls PH, Sternberg MJE. 1992. New algorithm to model protein-protein recognition based on surface complementarity. J Mol Biol 228:277-297.
    • (1992) J Mol Biol , vol.228 , pp. 277-297
    • Walls, P.H.1    Sternberg, M.J.E.2
  • 43
    • 0028212643 scopus 로고
    • Autonomous subdomains in protein folding
    • Wu LC, Grandori R, Carey J. 1994. Autonomous subdomains in protein folding. Protein Sci 3:359-371.
    • (1994) Protein Sci , vol.3 , pp. 359-371
    • Wu, L.C.1    Grandori, R.2    Carey, J.3
  • 44
    • 0031561809 scopus 로고    scopus 로고
    • Protein binding versus protein folding: The role of hydrophilic bridges in protein associations
    • Xu D, Lin SL, Nussinov R. 1997a. Protein binding versus protein folding: The role of hydrophilic bridges in protein associations. 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
  • 45
    • 0031450506 scopus 로고    scopus 로고
    • Hydrogen bonds and salt-bridges across protein-protein interfaces
    • in press
    • Xu D, Tsai C-J, Nussinov R. 1997b. Hydrogen bonds and salt-bridges across protein-protein interfaces. Protein Eng, in press.
    • (1997) Protein Eng
    • Xu, D.1    Tsai, C.-J.2    Nussinov, R.3
  • 46
    • 0028332007 scopus 로고
    • A role for surface hydrophobicity in protein-protein recognition
    • Young L, Jernigan RL, Covell DG. 1994. A role for surface hydrophobicity in protein-protein recognition. Protein Sci 3:717-729.
    • (1994) Protein Sci , vol.3 , pp. 717-729
    • Young, L.1    Jernigan, R.L.2    Covell, D.G.3
  • 47
    • 0027297660 scopus 로고
    • Improved calculations of compactness and a reevaluation of continuous compact units
    • Zehfus MH. 1993. Improved calculations of compactness and a reevaluation of continuous compact units. Proteins 76:293-300.
    • (1993) Proteins , vol.76 , pp. 293-300
    • Zehfus, M.H.1
  • 48
    • 0023055758 scopus 로고
    • Compact units in proteins
    • Zehfus MH, Rose GD. 1986. Compact units in proteins. Biochemistry 25:5759-5765.
    • (1986) Biochemistry , vol.25 , pp. 5759-5765
    • Zehfus, M.H.1    Rose, G.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.