메뉴 건너뛰기




Volumn 5, Issue 3, 1998, Pages 369-376

How homologs can help to predict protein folds even though they cannot be predicted for individual sequences

Author keywords

Averaging of energy parameters; Energy calculations; Errors in energy parameters; Homologs; Protein fold prediction

Indexed keywords

AMINO ACID SEQUENCE; ANALYTICAL ERROR; COMPUTER SIMULATION; CONFERENCE PAPER; GENE MUTATION; MATHEMATICAL ANALYSIS; PREDICTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; SEQUENCE HOMOLOGY; THERMODYNAMICS;

EID: 0031752309     PISSN: 10665277     EISSN: None     Source Type: Journal    
DOI: 10.1089/cmb.1998.5.369     Document Type: Conference Paper
Times cited : (6)

References (19)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C.B. 1973. Principles that govern the folding of protein chains. Science 181, 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0025935158 scopus 로고
    • Patterns of divergence in homologous proteins as indicators of secondary and tertiary structure: The catalytic domain of protein kinases
    • Benner, S.A., and Gerloff, D. 1990. Patterns of divergence in homologous proteins as indicators of secondary and tertiary structure: The catalytic domain of protein kinases. Adv. Enz. Reg. 31, 121-181.
    • (1990) Adv. Enz. Reg. , vol.31 , pp. 121-181
    • Benner, S.A.1    Gerloff, D.2
  • 3
    • 0025148817 scopus 로고
    • A simple statistical field-theory of heteropolymer collapse with application to protein folding
    • Bryngelson, J.B., and Wolynes, P.G. 1990. A simple statistical field-theory of heteropolymer collapse with application to protein folding. Biopolymers 30, 177-188.
    • (1990) Biopolymers , vol.30 , pp. 177-188
    • Bryngelson, J.B.1    Wolynes, P.G.2
  • 4
    • 4243861085 scopus 로고
    • Random-energy model: An exactly solvable model of disordered systems
    • Derrida, B. 1981. Random-energy model: An exactly solvable model of disordered systems. Phys. Rev. B24, 2613-2626.
    • (1981) Phys. Rev. , vol.B24 , pp. 2613-2626
    • Derrida, B.1
  • 5
    • 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, L.R. Jr., Gerloff, D.L., Bower, M., Chen, X., Lichtarge, O., and Cohen, F.E. 1997. Meeting review: The second meeting on the critical assessment of techniques for protein structure prediction (CASP2), Asilomar, California, December 13-16, 1996. Folding and Design 2, R27-R42.
    • (1997) Folding and Design , vol.2
    • Dunbrack Jr., L.R.1    Gerloff, D.L.2    Bower, M.3    Chen, X.4    Lichtarge, O.5    Cohen, F.E.6
  • 6
    • 0031043161 scopus 로고    scopus 로고
    • Nucleation mechanism in protein folding
    • Fersht, A.R. 1997. Nucleation mechanism in protein folding. Curr. Opin. Struct. Biol. 7, 3-9.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 3-9
    • Fersht, A.R.1
  • 7
    • 0028319316 scopus 로고
    • Implementation of the random characteristics of protein sequences for their three-dimensional structures
    • Finkelstein, A.V. 1994. Implementation of the random characteristics of protein sequences for their three-dimensional structures. Curr. Opin. Struct. Biol. 4, 422-428.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 422-428
    • Finkelstein, A.V.1
  • 8
    • 0031052179 scopus 로고    scopus 로고
    • Protein structure: What is possible to predict now?
    • Finkelstein, A.V. 1997. Protein structure: What is possible to predict now? Curr. Opin. Struct. Biol. 7, 60-71.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 60-71
    • Finkelstein, A.V.1
  • 9
    • 0001516165 scopus 로고    scopus 로고
    • 3D Protein folds: Homologs against errors, a simple estimate based on the random energy model
    • submitted
    • Finkelstein, A.V. 1998. 3D Protein folds: Homologs against errors, a simple estimate based on the random energy model. Phys. Rev. Lett., submitted.
    • (1998) Phys. Rev. Lett.
    • Finkelstein, A.V.1
  • 10
    • 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., and Badretdinov, A.Ya. 1997. Rate of protein folding near the point of thermodynamic equilibrium between the coil and the most stable chain fold. Folding and Design 2, 115-121.
    • (1997) Folding and Design , vol.2 , pp. 115-121
    • Finkelstein, A.V.1    Badretdinov, A.Ya.2
  • 11
    • 0028857906 scopus 로고
    • Perfect temperature for protein structure prediction and folding
    • Finkelstein, A.V., Gutin, A.M., and Badretdinov, A.Ya. 1995. Perfect temperature for protein structure prediction and folding. Proteins 23, 151-162.
    • (1995) Proteins , vol.23 , pp. 151-162
    • Finkelstein, A.V.1    Gutin, A.M.2    Badretdinov, A.Ya.3
  • 13
    • 0030631103 scopus 로고    scopus 로고
    • Simultaneous and coupled energy optimization of homologous proteins: A new tool for structure prediction
    • Keasar, C., Elber, R., and Skolnick, J. 1997. Simultaneous and coupled energy optimization of homologous proteins: A new tool for structure prediction. Folding and Design 2, 247-259.
    • (1997) Folding and Design , vol.2 , pp. 247-259
    • Keasar, C.1    Elber, R.2    Skolnick, J.3
  • 14
    • 0018796254 scopus 로고
    • Improvements in the prediction of protein backbone topography by reduction of statistical errors
    • Maxfield, F.R., and Scheraga, H.A. 1979. Improvements in the prediction of protein backbone topography by reduction of statistical errors. Biochemistry 18, 697-704.
    • (1979) Biochemistry , vol.18 , pp. 697-704
    • Maxfield, F.R.1    Scheraga, H.A.2
  • 15
    • 0032571390 scopus 로고    scopus 로고
    • Fold assembly of small proteins using Monte Carlo simulations driven by restraints derived from multiple sequence alignments
    • in press
    • Ortiz, A.R., Kolinsky, A., and Skolnick, J. 1998. Fold assembly of small proteins using Monte Carlo simulations driven by restraints derived from multiple sequence alignments. J. Mol. Biol., in press.
    • (1998) J. Mol. Biol.
    • Ortiz, A.R.1    Kolinsky, A.2    Skolnick, J.3
  • 17
    • 0024357911 scopus 로고
    • Formation of unique structure in polypeptide chains. Theoretical investigation with the aid of a replica approach
    • Shakhnovich, E.I., and Gutin, A.M. 1989. Formation of unique structure in polypeptide chains. Theoretical investigation with the aid of a replica approach. Biophys. Chem. 34, 187-199.
    • (1989) Biophys. Chem. , vol.34 , pp. 187-199
    • Shakhnovich, E.I.1    Gutin, A.M.2
  • 18
    • 36549097257 scopus 로고
    • Enumeration of all compact conformations of copolymers with random sequence of links
    • Shakhnovich, E.I., and Gutin, A.M. 1990. Enumeration of all compact conformations of copolymers with random sequence of links. J. Chem. Phys. 93, 5967-5971.
    • (1990) J. Chem. Phys. , vol.93 , pp. 5967-5971
    • Shakhnovich, E.I.1    Gutin, A.M.2
  • 19
    • 0030979740 scopus 로고    scopus 로고
    • Folding funnels and energy landscapes of larger protein within the capillarity approximation
    • Wolynes, P.G. 1997. Folding funnels and energy landscapes of larger protein within the capillarity approximation. Proc. Natl. Acad. Sci. USA 94, 6170-6175.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6170-6175
    • Wolynes, P.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.