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Volumn 1278, Issue , 1997, Pages 125-136

Simple folding model for HP lattice proteins

Author keywords

[No Author keywords available]

Indexed keywords

BIOINFORMATICS; BIOPOLYMERS; CHAINS; POLYPEPTIDES; PROTEINS;

EID: 84961341319     PISSN: 03029743     EISSN: 16113349     Source Type: Book Series    
DOI: None     Document Type: Conference Paper
Times cited : (5)

References (35)
  • 1
    • 0027491725 scopus 로고
    • Structural argument for N-terminal initiation of protein folding
    • N. Alexandrov. Structural argument for N-terminal initiation of protein folding. Protein Science, 2:1989-1991, 1993.
    • (1993) Protein Science , vol.2 , pp. 1989-1991
    • Alexandrov, N.1
  • 3
    • 0029896217 scopus 로고    scopus 로고
    • Random structures and evolution of biopolymers: A computational case study on RNA secondary structures
    • E. Bornberg-Bauer. Random structures and evolution of biopolymers: A computational case study on RNA secondary structures. Pharmaceutica Acta Helvetiae, 71(l):79-85, 1996.
    • (1996) Pharmaceutica Acta Helvetiae , vol.71 , Issue.1 , pp. 79-85
    • Bornberg-Bauer, E.1
  • 4
    • 0030309351 scopus 로고    scopus 로고
    • Structure formation of biopolymers is complex, their evolution may be simple
    • In L. Hunter and T. Klein, editors, World Scientific, London
    • E. Bornberg-Bauer. Structure formation of biopolymers is complex, their evolution may be simple. In L. Hunter and T. Klein, editors, Proceedings of the Pacific Symposium on Biocomputing, pages 97-108. World Scientific, London, 1996.
    • (1996) Proceedings of the Pacific Symposium on Biocomputing , pp. 97-108
    • Bornberg-Bauer, E.1
  • 5
    • 0003155594 scopus 로고    scopus 로고
    • Compelling folding codes for proteins and polymers
    • H. S. Chan and K. A. Dill. Compelling folding codes for proteins and polymers. Proteins, 24:335-344, 1996.
    • (1996) Proteins , vol.24 , pp. 335-344
    • Chan, H.S.1    Dill, K.A.2
  • 6
    • 0027122748 scopus 로고
    • One thousand families for the molecular biologist
    • C. Chothia. One thousand families for the molecular biologist. Nature, 357:543-544, 1992.
    • (1992) Nature , vol.357 , pp. 543-544
    • Chothia, C.1
  • 8
    • 84986524621 scopus 로고
    • X-ploring extraribosomal peptide folding during synthesis
    • C. W. David. X-ploring extraribosomal peptide folding during synthesis. J. Comp. Chem., 15:662-665, 1994.
    • (1994) J. Comp. Chem , vol.15 , pp. 662-665
    • David, C.W.1
  • 10
    • 0000381972 scopus 로고
    • Protein core assembly process
    • K. M. Fiebig and K. A. Dill. Protein core assembly process. J. Chem. Phys., 98:3475-3487, 1993.
    • (1993) J. Chem. Phys , vol.98 , pp. 3475-3487
    • Fiebig, K.M.1    Dill, K.A.2
  • 12
    • 0027692037 scopus 로고
    • Complexity of protein folding
    • A. Frænkel. Complexity of protein folding. Bull. Math. Biol., 55:1199-1210, 1993.
    • (1993) Bull. Math. Biol , vol.55 , pp. 1199-1210
    • Frænkel, A.1
  • 13
    • 36149033505 scopus 로고
    • Guided replication of random chains: A new monte carlo method
    • T. Garel and H. Orland. Guided replication of random chains: a new monte carlo method. J. Phys. A: Math. Gen., 23:L621-L626, 1990.
    • (1990) J. Phys. A: Math. Gen , vol.23 , pp. L621-L626
    • Garel, T.1    Orland, H.2
  • 14
    • 0030015087 scopus 로고    scopus 로고
    • Fast protein folding in the hydrophobic-hydrophilic model within three-eighths of optimal
    • W, E. Hart and S. C. Istrail. Fast protein folding in the hydrophobic-hydrophilic model within three-eighths of optimal. J. Comp. Biol., 3:53-96, 1996.
    • (1996) J. Comp. Biol , vol.3 , pp. 53-96
    • Hart, W.E.1    Istrail, S.C.2
  • 16
    • 0024750637 scopus 로고
    • A lattice statistical mechanics model of the conformational and sequence spaces of proteins
    • K. F. Lau and K. 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
  • 17
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • C. Levinthal. Are there pathways for protein folding? J. Chim. Phys., 65:44-45, 1968.
    • (1968) J. Chim. Phys , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 18
    • 0029772552 scopus 로고    scopus 로고
    • Emergence of preferred structures in a simple model of protein folding
    • H. Li, R. Helling, C. Tang, and N. Wingreen. Emergence of preferred structures in a simple model of protein folding. Science, 273:666-669, 1996.
    • (1996) Science , vol.273 , pp. 666-669
    • Li, H.1    Helling, R.2    Tang, C.3    Wingreen, N.4
  • 19
    • 0030025303 scopus 로고    scopus 로고
    • Enzymatic activity of the ribosome-bound nascent polypeptide
    • E. V. Makeyev, V. A. Kolb, and A. S. Spirin. Enzymatic activity of the ribosome-bound nascent polypeptide. FEBS Letters, 378:166-170, 1996.
    • (1996) FEBS Letters , vol.378 , pp. 166-170
    • Makeyev, E.V.1    Kolb, V.A.2    Spirin, A.S.3
  • 20
    • 0000614977 scopus 로고
    • Computer simulation of self-avoiding walks: Testing the scanning method
    • H. Meirovitch. Computer simulation of self-avoiding walks: Testing the scanning method. J. Chem. Phys., 79:502-508, 1983.
    • (1983) J. Chem. Phys , vol.79 , pp. 502-508
    • Meirovitch, H.1
  • 21
    • 0026776874 scopus 로고
    • Computational complexity of a problem in molecular structure prediction
    • J. T. Ngo and J. Marks. Computational complexity of a problem in molecular structure prediction. Protein Eng., 5:313-321, 1992.
    • (1992) Protein Eng , vol.5 , pp. 313-321
    • Ngo, J.T.1    Marks, J.2
  • 22
    • 0000669827 scopus 로고
    • Monte carlo simulation of folding transitions of simple model proteins using a chain growth algorithm
    • E. M. O'Toole and A. Z. Panagiotopoulos. Monte carlo simulation of folding transitions of simple model proteins using a chain growth algorithm. J. Chem. Phys., 97:8644-8652, 1992.
    • (1992) J. Chem. Phys , vol.97 , pp. 8644-8652
    • O'Toole, E.M.1    Panagiotopoulos, A.Z.2
  • 23
    • 0029063717 scopus 로고    scopus 로고
    • The complexity and accuracy of discrete state models. of protein structure
    • B. H. Park and M. Levitt. The complexity and accuracy of discrete state models. of protein structure. J. Mol. Biol., 249:493-507, 1996.
    • (1996) J. Mol. Biol , vol.249 , pp. 493-507
    • Park, B.H.1    Levitt, M.2
  • 24
    • 84961304073 scopus 로고    scopus 로고
    • Exploring the fitness landscapes of lattice proteins
    • In L. Hunter and T. Klein, editors, World Scientific, London, in press
    • A. Renner and E. Bornberg-Bauer. Exploring the fitness landscapes of lattice proteins. In L. Hunter and T. Klein, editors, Proceedings of the Pacific Symposium on Biocomputing. World Scientific, London, in press.
    • Proceedings of the Pacific Symposium on Biocomputing
    • Renner, A.1    Bornberg-Bauer, E.2
  • 26
    • 0028196714 scopus 로고
    • From sequences to shapes and back: A case study in RNA secondary structures
    • P. Schuster, W. Fontana, P. F. Stadler, and I. L. Hofacker. From sequences to shapes and back: A case study in RNA secondary structures. Proc.Roy.Sac.(London)B, 255:279-284, 1994.
    • (1994) Proc.Roy.Sac.(London)B , vol.255 , pp. 279-284
    • Schuster, P.1    Fontana, W.2    Stadler, P.F.3    Hofacker, I.L.4
  • 27
    • 0002698766 scopus 로고    scopus 로고
    • Modeling protein folding: The beauty and power of simplicity
    • E. I. Shakhnovich. Modeling protein folding: the beauty and power of simplicity. Folding & Design, 1:R50-R54, 1996.
    • (1996) Folding & Design , vol.1 , pp. R50-R54
    • Shakhnovich, E.I.1
  • 28
    • 0028887914 scopus 로고
    • Exploration of compact protein conformations using the guided replication monte carlo method
    • J. E. Solomon and D. Liney. Exploration of compact protein conformations using the guided replication monte carlo method. Biopolymers, 36:579-597, 1995.
    • (1995) Biopolymers , vol.36 , pp. 579-597
    • Solomon, J.E.1    Liney, D.2
  • 30
    • 0030018101 scopus 로고    scopus 로고
    • Ribosome-mediated translation pause and protein domain organization
    • T. Thanaraj and P. Argos. Ribosome-mediated translation pause and protein domain organization. Protein Science, 5:1594-1612, 1996.
    • (1996) Protein Science , vol.5 , pp. 1594-1612
    • Thanaraj, T.1    Argos, P.2
  • 31
    • 0027690211 scopus 로고
    • Finding lowest free energy conformation of a protein is an NP-hard problem: Proof and implications
    • R. Unger and J. Moult. Finding lowest free energy conformation of a protein is an NP-hard problem: Proof and implications. Bull. Math. Biol., 55:1183-1198, 1993.
    • (1993) Bull. Math. Biol , vol.55 , pp. 1183-1198
    • Unger, R.1    Moult, J.2
  • 32
    • 0027245418 scopus 로고
    • Genetic algorithms for protein folding simulations
    • R. Unger and J. Moult. Genetic algorithms for protein folding simulations. J. Mol. Biol., 231:75-81, 1993.
    • (1993) J. Mol. Biol , vol.231 , pp. 75-81
    • Unger, R.1    Moult, J.2
  • 33
    • 0021813809 scopus 로고
    • Use of buildup and energy-minimization procedures to compute low-energy structures of the backbone of enkephalin
    • M. Vasquez and H. A. Scheraga. Use of buildup and energy-minimization procedures to compute low-energy structures of the backbone of enkephalin. Biopolymers, 24:1437-1447, 1985.
    • (1985) Biopolymers , vol.24 , pp. 1437-1447
    • Vasquez, M.1    Scheraga, H.A.2
  • 34
    • 0015597839 scopus 로고
    • Nucleation, rapid folding and globular intrachain regions in proteins
    • D. B. Wetlaufer. Nucleation, rapid folding and globular intrachain regions in proteins. Proc. Natl. Acad. Sci., USA, 70:697-701, 1973.
    • (1973) Proc. Natl. Acad. Sci., USA , vol.70 , pp. 697-701
    • Wetlaufer, D.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.