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Volumn 1520, Issue , 1998, Pages 72-86

Constraint techniques for solving the protein structure prediction problem

Author keywords

[No Author keywords available]

Indexed keywords

BIOINFORMATICS; COMPUTER PROGRAMMING; CONSTRAINT THEORY; FORECASTING;

EID: 84957682501     PISSN: 03029743     EISSN: 16113349     Source Type: Book Series    
DOI: 10.1007/3-540-49481-2_7     Document Type: Conference Paper
Times cited : (14)

References (19)
  • 1
    • 0029155772 scopus 로고
    • Impact of local and nonlocal interactions on thermodynamics and kinetics of protein folding
    • V. I. Abkevich, A. M. Gutin, and E. I. Shakhnovich. Impact of local and nonlocal interactions on thermodynamics and kinetics of protein folding. Journal of Molecular Biology, 252:460-471, 1995.
    • (1995) Journal of Molecular Biology , vol.252 , pp. 460-471
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 2
    • 0031300842 scopus 로고    scopus 로고
    • Computer simulations of prebiotic evolution
    • Russ B. Altman, A. Keith Dunker, Lawrence Hunter, and Teri E. Klein, editors
    • V.I. Abkevich, A.M. Gutin, and E.I. Shakhnovich. Computer simulations of prebiotic evolution. In Russ B. Altman, A. Keith Dunker, Lawrence Hunter, and Teri E. Klein, editors, PSB'97, pages 27-38, 1997.
    • (1997) PSB'97 , pp. 27-38
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 3
    • 0031685674 scopus 로고    scopus 로고
    • Protein folding in the hydrophobic-hydrophilic (HP) modell is NP-complete
    • B. Berger and T. Leighton. Protein folding in the hydrophobic-hydrophilic (HP) modell is NP-complete. In Proc. of the RECOMB'98, pages 30-39, 1998.
    • (1998) Proc. of the RECOMB'98 , pp. 30-39
    • Berger, B.1    Leighton, T.2
  • 8
    • 0029781355 scopus 로고    scopus 로고
    • The folding mechanism of larger model proteins: Role of native structure
    • Aaron R. Dinner, Andreaj Šali, and Martin Karplus. The folding mechanism of larger model proteins: Role of native structure. Proc. Natl. Acad. Sci. USA, 93:8356-8361, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8356-8361
    • Dinner, A.R.1    Šali, R.2    Karplus, M.3
  • 9
    • 0031555012 scopus 로고    scopus 로고
    • The foldability landscape of model proteins
    • S. Govindarajan and R. A. Goldstein. The foldability landscape of model proteins. Biopolymers, 42(4):427-438, 1997.
    • (1997) Biopolymers , vol.42 , Issue.4 , pp. 427-438
    • Govindarajan, S.1    Goldstein, R.A.2
  • 10
    • 0030015087 scopus 로고    scopus 로고
    • Fast protein folding in the hydrophobidhydrophilic model within three-eighths of optimal
    • William E. Hart and Sorin C. Istrail. Fast protein folding in the hydrophobidhydrophilic model within three-eighths of optimal. Journal of Computational Bi- ology, 3(1):53-96, 1996.
    • (1996) Journal of Computational Bi- Ology , vol.3 , Issue.1 , pp. 53-96
    • Hart, W.E.1    Istrail, S.C.2
  • 11
    • 0029883960 scopus 로고    scopus 로고
    • Hinds and Michael Levitt. From structure to sequence and back again
    • David A. Hinds and Michael Levitt. From structure to sequence and back again. Journal of Molecular Biology, 258:201-209, 1996.
    • (1996) Journal of Molecular Biology , vol.258 , pp. 201-209
    • David, A.1
  • 12
    • 0024750637 scopus 로고
    • A lattice statistical mechanics model of the conformational and sequence spaces of proteins
    • Kit Fun Lau and Ken A. Dill. A lattice statistical mechanics model of the conformational and sequence spaces of proteins. Macromolecules, 22:3986-3997, 1989.
    • (1989) Macromolecules , vol.22 , pp. 3986-3997
    • Lau, K.F.1    Dill, K.A.2
  • 13
    • 0031630501 scopus 로고    scopus 로고
    • Combined multiple sequence reduced protein model approach to predict the tertiary structure of small proteins
    • Russ B. Altman, A. Keith Dunker, Lawrence Hunter, and Teri E. Klein, editors
    • Angel R. Ortiz, Andrzej Kolinski, and Jeffrey Skolnick. Combined multiple sequence reduced protein model approach to predict the tertiary structure of small proteins. In Russ B. Altman, A. Keith Dunker, Lawrence Hunter, and Teri E. Klein, editors, PSB'98, volume 3, pages 375-386, 1998.
    • (1998) PSB'98, Volume 3 , pp. 375-386
    • Ortiz, A.R.1    Kolinski, R.2    Skolnick, J.3
  • 14
    • 0000777964 scopus 로고
    • The Oz programming model
    • In Jan van Leeuwen, editor, Springer-Verlag, Berlin
    • Gert Smolka. The Oz programming model. In Jan van Leeuwen, editor, Com- puter Science Today, Lecture Notes in Computer Science, vol. 1000, pages 324-343. Springer-Verlag, Berlin, 1995.
    • (1995) Com- Puter Science Today, Lecture Notes in Computer Science , vol.1000 , pp. 324-343
    • Smolka, G.1
  • 15
    • 0027245418 scopus 로고
    • Genetic algorithms for protein folding simulations
    • R. Unger and J. Moult. Genetic algorithms for protein folding simulations. Journal of Molecular Biology, 231:75-81, 1993.
    • (1993) Journal of Molecular Biology , vol.231 , pp. 75-81
    • Unger, R.1    Moult, J.2
  • 16
    • 0030604696 scopus 로고    scopus 로고
    • Local interactions dominate folding in a simple protein model
    • Ron Unger and John Moult. Local interactions dominate folding in a simple protein model. Journal of Molecular Biology, 259:988-994, 1996.
    • (1996) Journal of Molecular Biology , vol.259 , pp. 988-994
    • Unger, R.1    Moult, J.2
  • 18
    • 0001747878 scopus 로고
    • Sequence-structure relationships in proteins and copolymers
    • September
    • Kaizhi Yue and Ken A. Dill. Sequence-structure relationships in proteins and copolymers. Physical Review E, 48(3):2267-2278, September 1993.
    • (1993) Physical Review E , vol.48 , Issue.3 , pp. 2267-2278
    • Yue, K.1    Dill, K.A.2
  • 19
    • 0028950075 scopus 로고
    • Forces of tertiary structural organization in globular proteins
    • Kaizhi Yue and Ken A. Dill. Forces of tertiary structural organization in globular proteins. Proc. Natl. Acad. Sci. USA, 92:146-150, 1995.
    • (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.