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Volumn 5, Issue 2, 1996, Pages 254-261

Folding proteins with a simple energy function and extensive conformational searching

Author keywords

conformational search; energy potential; protein folding; structure prediction

Indexed keywords

APAMIN; MELITTIN; PANCREAS POLYPEPTIDE;

EID: 0030048675     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050209     Document Type: Article
Times cited : (75)

References (36)
  • 2
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB. 1973. Principles that govern the folding of protein chains. Science 181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 4
    • 0029151245 scopus 로고
    • First-principles calculation of the folding free energy of a three-helix bundle protein
    • Boczko EM, Brooks CL. 1995. First-principles calculation of the folding free energy of a three-helix bundle protein. Science 269:393-396.
    • (1995) Science , vol.269 , pp. 393-396
    • Boczko, E.M.1    Brooks, C.L.2
  • 6
    • 0026761547 scopus 로고
    • Folding protein α-carbon chains into compact forms by Monte Carlo methods
    • Covell DG. 1992. Folding protein α-carbon chains into compact forms by Monte Carlo methods. Proteins Struct Funct Genet 14:409-420.
    • (1992) Proteins Struct Funct Genet , vol.14 , pp. 409-420
    • Covell, D.G.1
  • 7
    • 0028049306 scopus 로고
    • Lattice model simulations of polypeptide chain folding
    • Covell DG. 1994. Lattice model simulations of polypeptide chain folding. J Mol Biol 235:1032-1043.
    • (1994) J Mol Biol , vol.235 , pp. 1032-1043
    • Covell, D.G.1
  • 8
    • 0026777802 scopus 로고
    • Representation of noncovalent interactions in protein structures
    • De la Cruz X, Reverter J, Fita I. 1992. Representation of noncovalent interactions in protein structures. J Mol Graphics 10:96-110.
    • (1992) J Mol Graphics , vol.10 , pp. 96-110
    • De La Cruz, X.1    Reverter, J.2    Fita, I.3
  • 9
    • 0000669847 scopus 로고
    • Molecular orbital theory of the hydrogen bond. XII
    • Del Bene J. 1975. Molecular orbital theory of the hydrogen bond. XII. J Chem Phys 62:1961-1970.
    • (1975) J Chem Phys , vol.62 , pp. 1961-1970
    • Del Bene, J.1
  • 10
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA. 1990. Dominant forces in protein folding. Biochemistry 29:7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 14
    • 0028149160 scopus 로고
    • Exploring conformational space with a simple lattice model for protein structure
    • Hinds D, Levitt M. 1994. Exploring conformational space with a simple lattice model for protein structure. J Mol Biol 243:668-682.
    • (1994) J Mol Biol , vol.243 , pp. 668-682
    • Hinds, D.1    Levitt, M.2
  • 16
    • 0028203492 scopus 로고
    • Monte Carlo simulations of protein folding. I. Lattice model and interaction scheme
    • Kolinski A, Skolnick J. 1994. Monte Carlo simulations of protein folding. I. Lattice model and interaction scheme. Proteins Struct Funct Genet 18:338-352.
    • (1994) Proteins Struct Funct Genet , vol.18 , pp. 338-352
    • Kolinski, A.1    Skolnick, J.2
  • 18
    • 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
  • 19
    • 0001840852 scopus 로고
    • Directional character, strength, and nature of the hydrogen bond in gas phase dimers
    • Legon AC, Millen DJ. 1987. Directional character, strength, and nature of the hydrogen bond in gas phase dimers. Acc Chem Res 20:39-45.
    • (1987) Acc Chem Res , vol.20 , pp. 39-45
    • Legon, A.C.1    Millen, D.J.2
  • 20
    • 0016610491 scopus 로고
    • Computer simulation of protein folding
    • Levitt M, Warshel A. 1975. Computer simulation of protein folding. Nature 253:694-698.
    • (1975) Nature , vol.253 , pp. 694-698
    • Levitt, M.1    Warshel, A.2
  • 21
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald I, Thornton J. 1994. Satisfying hydrogen bonding potential in proteins. J Mol Biol 238:777-793.
    • (1994) J Mol Biol , vol.238 , pp. 777-793
    • McDonald, I.1    Thornton, J.2
  • 22
    • 33845377127 scopus 로고
    • Estimation of effective interresidue contact energies from protein crystal structures: Quasi-chemical approximation
    • Miyazawa S, Jernigan RL. 1985. Estimation of effective interresidue contact energies from protein crystal structures: Quasi-chemical approximation. Macromolecule 18:534-552.
    • (1985) Macromolecule , vol.18 , pp. 534-552
    • Miyazawa, S.1    Jernigan, R.L.2
  • 23
    • 0028283339 scopus 로고
    • An algorithm to generate low-resolution protein tertiary structures from knowledge of secondary structure
    • Monge A, Friesner RA, Honig B. 1994. An algorithm to generate low-resolution protein tertiary structures from knowledge of secondary structure. Proc Natl Acad Sci USA 91:5027-5029.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5027-5029
    • Monge, A.1    Friesner, R.A.2    Honig, B.3
  • 24
    • 0023804632 scopus 로고
    • Criteria that discriminate between native proteins and incorrectly folded models
    • Novotny J, Rashin AA, Bruccoleri RE. 1988. Criteria that discriminate between native proteins and incorrectly folded models. Proteins Struct Funct Genet 4:19-30.
    • (1988) Proteins Struct Funct Genet , vol.4 , pp. 19-30
    • Novotny, J.1    Rashin, A.A.2    Bruccoleri, R.E.3
  • 25
    • 0026416668 scopus 로고
    • Reconciling the magnitude of the microscopic and macroscopic hydrophobic effects
    • Sharp K, Nicholls A, Fine RF, Honig B. 1991. Reconciling the magnitude of the microscopic and macroscopic hydrophobic effects. Science 252: 106.
    • (1991) Science , vol.252 , pp. 106
    • Sharp, K.1    Nicholls, A.2    Fine, R.F.3    Honig, B.4
  • 26
    • 0027055791 scopus 로고
    • Assembly of polypeptide and protein backbone conformations from low energy ensembles of short fragments: Development of strategies and construction of models for myoglobin, lysozyme, and thymosin beta 4
    • Sippl M, Hendlich M, Lackner P. 1992. Assembly of polypeptide and protein backbone conformations from low energy ensembles of short fragments: Development of strategies and construction of models for myoglobin, lysozyme, and thymosin beta 4. Protein Sci 1:625-640.
    • (1992) Protein Sci , vol.1 , pp. 625-640
    • Sippl, M.1    Hendlich, M.2    Lackner, P.3
  • 27
    • 0025608908 scopus 로고
    • Simulations of the folding of a globular protein
    • Skolnick J, Kolinski A. 1990. Simulations of the folding of a globular protein. Science 250:1121-1125.
    • (1990) Science , vol.250 , pp. 1121-1125
    • Skolnick, J.1    Kolinski, A.2
  • 28
    • 0029055313 scopus 로고
    • LINUS - A hierarchic procedure to predict the fold of a protein
    • Srinivasan R, Rose G. 1995. LINUS - A hierarchic procedure to predict the fold of a protein. Proteins Struct Funct Genet 22:81-99.
    • (1995) Proteins Struct Funct Genet , vol.22 , pp. 81-99
    • Srinivasan, R.1    Rose, G.2
  • 29
    • 0028841399 scopus 로고
    • A simple protein folding algorithm using a binary code and secondary structure constraints
    • Forthcoming
    • Sun S, Thomas PD, Dill KA. 1995. A simple protein folding algorithm using a binary code and secondary structure constraints. Protein Eng. Forthcoming.
    • (1995) Protein Eng.
    • Sun, S.1    Thomas, P.D.2    Dill, K.A.3
  • 30
    • 21844437785 scopus 로고
    • Hydrogen bond geometry in organic crystals
    • Taylor R, Kennard O. 1984. Hydrogen bond geometry in organic crystals. Acc Chem Res 17:320-326.
    • (1984) Acc Chem Res , vol.17 , pp. 320-326
    • Taylor, R.1    Kennard, O.2
  • 31
    • 0027458546 scopus 로고
    • Necessary conditions for avoiding incorrect polypeptide folds in conformational search by energy minimization
    • Vajda S, Jafri MS, Sezerman OU, DeLisi C. 1993. Necessary conditions for avoiding incorrect polypeptide folds in conformational search by energy minimization. Biopolymers 33:173-192.
    • (1993) Biopolymers , vol.33 , pp. 173-192
    • Vajda, S.1    Jafri, M.S.2    Sezerman, O.U.3    Delisi, C.4
  • 32
    • 0028347939 scopus 로고
    • A simplified amino acid potential for use in structure predictions of proteins
    • Wallqvist A, Ullner M. 1994. A simplified amino acid potential for use in structure predictions of proteins. Proteins Struct Funct Genet 18:267-280.
    • (1994) Proteins Struct Funct Genet , vol.18 , pp. 267-280
    • Wallqvist, A.1    Ullner, M.2
  • 33
    • 0024435638 scopus 로고
    • A computer model to dynamically simulate protein folding - Studies with crambin
    • Wilson C, Doniach S. 1989. A computer model to dynamically simulate protein folding - Studies with crambin. Proteins Struct Fund Genet 6:193-209.
    • (1989) Proteins Struct Fund Genet , vol.6 , pp. 193-209
    • Wilson, C.1    Doniach, S.2
  • 34
    • 0001747878 scopus 로고
    • Sequence structure relationship of proteins and copolymers
    • Yue K, Dill KA. 1993. Sequence structure relationship of proteins and copolymers. Phys Rev E 48:2267-2278.
    • (1993) Phys Rev E , vol.48 , pp. 2267-2278
    • Yue, K.1    Dill, K.A.2
  • 35
    • 0028950075 scopus 로고
    • Forces of tertiary structural organization of globular proteins
    • Yue K, Dill KA. 1995. Forces of tertiary structural organization of 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.