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Volumn 25, Issue 1-2, 2003, Pages 139-159

Long proteins with unique optimal foldings in the H-P model

Author keywords

Combinatorial geometry; Energy minimization; Folding stability; Hydrophobic hydrophilic model; Protein folding

Indexed keywords


EID: 84867973812     PISSN: 09257721     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0925-7721(02)00134-7     Document Type: Conference Paper
Times cited : (18)

References (38)
  • 4
    • 78449300388 scopus 로고
    • Studies on the principles that govern the folding of protein chains
    • Nobel Foundation
    • C. Anfinsen Studies on the principles that govern the folding of protein chains Les Prix Nobel en 1972 1972 Nobel Foundation 103 119
    • (1972) Les Prix Nobel en 1972 , pp. 103-119
    • Anfinsen, C.1
  • 7
    • 84937391336 scopus 로고    scopus 로고
    • An upper bound for number of contacts in the HP-model on the face-centered-cubic lattice (FCC)
    • Lecture Notes in Computer Science
    • R. Backofen An upper bound for number of contacts in the HP-model on the face-centered-cubic lattice (FCC) Proceedings of the 11th Annual Symposium on Combinatorial Pattern Matching, Montreal Lecture Notes in Computer Science 1848 2000 277 292
    • (2000) Proceedings of the 11th Annual Symposium on Combinatorial Pattern Matching, Montreal , vol.1848 , pp. 277-292
    • Backofen, R.1
  • 9
    • 0031897962 scopus 로고    scopus 로고
    • Protein folding in the hydrophobic-hydrophilic (HP) model is NP-complete
    • B. Berger, and T. Leighton Protein folding in the hydrophobic-hydrophilic (HP) model is NP-complete J. Comput. Biology 5 1 1998 27 40
    • (1998) J. Comput. Biology , vol.5 , Issue.1 , pp. 27-40
    • Berger, B.1    Leighton, T.2
  • 12
    • 0025150383 scopus 로고
    • Origins of structure in globular proteins
    • H.S. Chan, and K.A. Dill Origins of structure in globular proteins Proc. Nat. Acad. Sci. USA 87 1990 6388 6392
    • (1990) Proc. Nat. Acad. Sci. USA , vol.87 , pp. 6388-6392
    • Chan, H.S.1    Dill, K.A.2
  • 14
    • 0000868733 scopus 로고
    • The protein folding problem
    • H.S. Chan, and K.A. Dill The protein folding problem Physics Today February 1993 24 32
    • (1993) Physics Today , pp. 24-32
    • Chan, H.S.1    Dill, K.A.2
  • 17
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • K.A. Dill Dominant forces in protein folding Biochemistry 29 31 1990 7133 7155
    • (1990) Biochemistry , vol.29 , Issue.31 , pp. 7133-7155
    • Dill, K.A.1
  • 23
    • 84872701755 scopus 로고
    • On the number of trees in Z d
    • E.J. Janse Van Rensburg On the number of trees in Z d J. Phys. A 25 1992 3523 3528
    • (1992) J. Phys. A , vol.25 , pp. 3523-3528
    • Janse Van Rensburg, E.J.1
  • 24
    • 0035534202 scopus 로고    scopus 로고
    • Enumerations of lattice animals and trees
    • I. Jensen Enumerations of lattice animals and trees J. Statist. Phys. 102 3-4 2001 865 881
    • (2001) J. Statist. Phys. , vol.102 , Issue.34 , pp. 865-881
    • Jensen, I.1
  • 26
    • 0024750637 scopus 로고
    • A lattice statistical mechanics model of the conformation and sequence spaces of proteins
    • K.F. Lau, and K.A. Dill A lattice statistical mechanics model of the conformation and sequence spaces of proteins Macromolecules 22 1989 3986 3997
    • (1989) Macromolecules , vol.22 , pp. 3986-3997
    • Lau, K.F.1    Dill, K.A.2
  • 27
    • 0025101549 scopus 로고
    • Theory for protein mutability and biogenesis
    • K.F. Lau, and K.A. Dill Theory for protein mutability and biogenesis Proc. Nat. Acad. Sci. USA 87 1990 638 642
    • (1990) Proc. Nat. Acad. Sci. USA , vol.87 , pp. 638-642
    • Lau, K.F.1    Dill, K.A.2
  • 28
    • 0025745163 scopus 로고
    • Modelling neutral and selective evolution of protein folding
    • D.J. Lipman, and W.J. Wilber Modelling neutral and selective evolution of protein folding Proc. Royal Soc. London, Ser. B 245 1312 1991 7 11
    • (1991) Proc. Royal Soc. London, Ser. B , vol.245 , Issue.1312 , pp. 7-11
    • Lipman, D.J.1    Wilber, W.J.2
  • 31
    • 0031236591 scopus 로고    scopus 로고
    • Molecular modeling of proteins and mathematical prediction of protein structure
    • A. Neumaier Molecular modeling of proteins and mathematical prediction of protein structure SIAM Rev. 39 3 1997 407 460
    • (1997) SIAM Rev. , vol.39 , Issue.3 , pp. 407-460
    • Neumaier, A.1
  • 34
    • 0027690211 scopus 로고
    • Finding the lowest free energy conformation of a protein is a NP-hard problem: Proof and implications
    • R. Unger, and J. Moult Finding the lowest free energy conformation of a protein is a NP-hard problem: Proof and implications Bull. Math. Biology 55 6 1993 1183 1198
    • (1993) Bull. Math. Biology , vol.55 , Issue.6 , pp. 1183-1198
    • Unger, R.1    Moult, J.2
  • 36
    • 0027245418 scopus 로고
    • Genetic algorithms for protein folding simulations
    • R. Unger, and J. Moult Genetic algorithms for protein folding simulations J. Molecular Biology 231 1 1993 75 81
    • (1993) J. Molecular Biology , vol.231 , Issue.1 , pp. 75-81
    • Unger, R.1    Moult, J.2
  • 38
    • 0028270634 scopus 로고
    • Kinetics of protein folding: A lattice model study of the requirements for folding to the native state
    • A. Šali, E. Shaknovich, and M. Karplus Kinetics of protein folding: A lattice model study of the requirements for folding to the native state J. Molecular Biology 235 1994 1614 1636
    • (1994) J. Molecular Biology , vol.235 , pp. 1614-1636
    • Šali, A.1    Shaknovich, E.2    Karplus, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.