메뉴 건너뛰기




Volumn 7, Issue 3, 1999, Pages 347-360

Design of sequences with good folding properties in coarse-grained protein models

Author keywords

Lattice models; Monte Carlo methods; Off lattice models, protein design; Protein folding

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; SYSTEM ANALYSIS; THERMODYNAMICS;

EID: 0033103164     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80044-6     Document Type: Article
Times cited : (35)

References (29)
  • 1
    • 0027438090 scopus 로고
    • A new approach to the design of stable proteins
    • Shakhnovich, E.I. & Gutin, A.M. (1993). A new approach to the design of stable proteins. Protein Eng. 6, 793-800
    • (1993) Protein Eng. , vol.6 , pp. 793-800
    • Shakhnovich, E.I.1    Gutin, A.M.2
  • 2
    • 0027234766 scopus 로고
    • Engineering of stable fast- folding sequences of model proteins
    • Shakhnovich, E.I. & Gutin, A.M. (1993). Engineering of stable fast- folding sequences of model proteins. Proc. Natl Acad. Sci. USA 90, 7195-7199.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7195-7199
    • Shakhnovich, E.I.1    Gutin, A.M.2
  • 3
    • 4243392673 scopus 로고
    • Proteins with selected sequences fold into unique native conformation
    • Shakhnovich, E.I. (1994). Proteins with selected sequences fold into unique native conformation. Phys. Rev. Lett. 72, 3907-3910.
    • (1994) Phys. Rev. Lett. , vol.72 , pp. 3907-3910
    • Shakhnovich, E.I.1
  • 4
    • 36149035731 scopus 로고
    • Design of copolymeric materials
    • Kurosky, T. & Deutsch, J.M. (1995). Design of copolymeric materials. J. Phys. A 27, L387-L393.
    • (1995) J. Phys. A , vol.27
    • Kurosky, T.1    Deutsch, J.M.2
  • 5
    • 4243719017 scopus 로고    scopus 로고
    • New algorithm for protein design
    • Deutsch, J.M. & Kurosky, T. (1996). New algorithm for protein design. Phys. Rev. Lett. 76, 323-326.
    • (1996) Phys. Rev. Lett. , vol.76 , pp. 323-326
    • Deutsch, J.M.1    Kurosky, T.2
  • 6
    • 0030322731 scopus 로고    scopus 로고
    • Design of proteins with selected thermal properties
    • Morrissey, M.P. & Shakhnovich, E.I. (1996). Design of proteins with selected thermal properties. Fold. Des. 1, 391-405.
    • (1996) Fold. Des. , vol.1 , pp. 391-405
    • Morrissey, M.P.1    Shakhnovich, E.I.2
  • 8
    • 0000773431 scopus 로고
    • Studies of an off-lattice model for protein folding: Sequence dependence and improved sampling at finite temperature
    • Irbäck, A. & Potthast, F. (1995). Studies of an off-lattice model for protein folding: Sequence dependence and improved sampling at finite temperature. J. Chem. Phys. 103, 10298-10305.
    • (1995) J. Chem. Phys. , vol.103 , pp. 10298-10305
    • Irbäck, A.1    Potthast, F.2
  • 10
    • 0024750637 scopus 로고
    • A lattice statistical model for the conformational and sequence spaces of proteins
    • Lau, K.F. & Dill, K.A. (1989). A lattice statistical model for the conformational and sequence spaces of proteins. Macromolecules 22, 3986-3997.
    • (1989) Macromolecules , vol.22 , pp. 3986-3997
    • Lau, K.F.1    Dill, K.A.2
  • 11
    • 0000699921 scopus 로고    scopus 로고
    • Local interactions and protein folding: A three-dimensional off-lattice approach
    • Irbäck, A., Peterson, C., Potthast, F. & Sommelius, O. (1997). Local interactions and protein folding: A three-dimensional off-lattice approach. J. Chem. Phys. 107, 273-282.
    • (1997) J. Chem. Phys. , vol.107 , pp. 273-282
    • Irbäck, A.1    Peterson, C.2    Potthast, F.3    Sommelius, O.4
  • 13
    • 33644899039 scopus 로고
    • Simulated tempering: A new monte carlo scheme
    • Marinari, E. & Parisi, G. (1992). Simulated tempering: A new monte carlo scheme. Europhys. Lett. 19, 451-458.
    • (1992) Europhys. Lett. , vol.19 , pp. 451-458
    • Marinari, E.1    Parisi, G.2
  • 14
    • 18844424885 scopus 로고    scopus 로고
    • Identification of amino acid sequences with good folding properties
    • Irbäck, A., Peterson, C. & Potthast, F. (1997). Identification of amino acid sequences with good folding properties. Phys. Rev. E 55, 860-867.
    • (1997) Phys. Rev. E , vol.55 , pp. 860-867
    • Irbäck, A.1    Peterson, C.2    Potthast, F.3
  • 15
    • 0002501593 scopus 로고    scopus 로고
    • Dynamical-parameter algorithms for protein folding
    • (Grassberger, P., Barkema, G. & Nadler, W., eds), World Scientific, Singapore.
    • Irbäck, A. Dynamical-parameter algorithms for protein folding. In Monte Carlo Approach to Biopolymers and Protein Folding. (Grassberger, P., Barkema, G. & Nadler, W., eds), p98-109, World Scientific, Singapore.
    • Monte Carlo Approach to Biopolymers and Protein Folding , pp. 98-109
    • Irbäck, A.1
  • 16
    • 0028950075 scopus 로고
    • Forces of tertiary structural organization in globular proteins
    • Yue, K. & Dill, K.A. (1995). Forces of tertiary structural organization in 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
  • 17
    • 0029772552 scopus 로고    scopus 로고
    • Emergence of preferred structures in a simple model of protein folding
    • Li, H., Helling, R., Tang, C. & Wingreen, N. (1996). Emergence of preferred structures in a simple model of protein folding. Science 273, 666-669.
    • (1996) Science , vol.273 , pp. 666-669
    • Li, H.1    Helling, R.2    Tang, C.3    Wingreen, N.4
  • 18
    • 36449000646 scopus 로고
    • Transition states and folding dynamics of proteins and heteropolymers
    • Chan, H.S. & Dill, K.A. (1994). Transition states and folding dynamics of proteins and heteropolymers. J. Chem. Phys. 100, 9238-9257.
    • (1994) J. Chem. Phys. , vol.100 , pp. 9238-9257
    • Chan, H.S.1    Dill, K.A.2
  • 19
    • 0000553651 scopus 로고    scopus 로고
    • Local interactions and protein folding: A model study on the square and triangular lattices
    • Irbäck, A. & Sandelin, E. (1998). Local interactions and protein folding: A model study on the square and triangular lattices. J. Phys. Chem. 108, 2245-2250.
    • (1998) J. Phys. Chem. , vol.108 , pp. 2245-2250
    • Irbäck, A.1    Sandelin, E.2
  • 20
    • 0002271227 scopus 로고
    • Monte carlo methods for the self-avoiding walk
    • (Binder, K., ed.), chapter 2, Oxford University Press, New York.
    • Sokal, A.D. (1995). Monte carlo methods for the self-avoiding walk. In Monte Carlo and Molecular Dynamics Simulations in Polymer Science. (Binder, K., ed.), chapter 2, Oxford University Press, New York.
    • (1995) Monte Carlo and Molecular Dynamics Simulations in Polymer Science
    • Sokal, A.D.1
  • 22
    • 0029155772 scopus 로고
    • Impact of local and non-local interactions on thermodynamics and kinetics of protein folding
    • Abkevich, V.I., Gutin, A.M. & Shakhnovich, E.I. (1995). Impact of local and non-local interactions on thermodynamics and kinetics of protein folding. J. Mol. Biol. 252, 460-471.
    • (1995) J. Mol. Biol. , vol.252 , pp. 460-471
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 23
    • 0031059496 scopus 로고    scopus 로고
    • Theoretical studies of protein-folding thermodynamics and kinetics
    • Shakhnovich, E.I. (1997). Theoretical studies of protein-folding thermodynamics and kinetics. Curr. Opin. Struct. Biol. 7, 29-40.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 29-40
    • Shakhnovich, E.I.1
  • 24
    • 0030624384 scopus 로고    scopus 로고
    • Protein folding kinetics: Timescales, pathways, and energy landscapes in terms of sequence-dependent properties
    • Veitshans, T., Klimov, D. & Thirumalai, D. (1997). Protein folding kinetics: Timescales, pathways, and energy landscapes in terms of sequence-dependent properties. Fold. Des. 2, 1-22.
    • (1997) Fold. Des. , vol.2 , pp. 1-22
    • Veitshans, T.1    Klimov, D.2    Thirumalai, D.3
  • 25
    • 0029114646 scopus 로고
    • Conformation, energy, and folding ability of selected amino acid sequences
    • Sasai, M. (1995). Conformation, energy, and folding ability of selected amino acid sequences. Proc. Natl Acad. Sci. USA 92, 8438-8442.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8438-8442
    • Sasai, M.1
  • 26
    • 0032568599 scopus 로고    scopus 로고
    • Folding funnels and frustration in off-lattice minimalist protein landscapes
    • Nymeyer, H., Garcia, A.E. & Onuchic, J.N. (1998). Folding funnels and frustration in off-lattice minimalist protein landscapes. Proc. Natl Acad. Sci. USA 95, 5921-5928.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5921-5928
    • Nymeyer, H.1    Garcia, A.E.2    Onuchic, J.N.3
  • 27
    • 0032169011 scopus 로고    scopus 로고
    • Proposed mechanism for stability of proteins to evolutionary mutations
    • Nelson, E.D. & Onuchic, J.N. (1998). Proposed mechanism for stability of proteins to evolutionary mutations. Proc. Natl Acad. Sci. USA 95, 10682-10686.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 10682-10686
    • Nelson, E.D.1    Onuchic, J.N.2
  • 28
    • 7044220745 scopus 로고    scopus 로고
    • Nature of driving force for protein folding: A result from analyzing the statistical potential
    • Li, H., Tang, C. & Wingreen, N.S. (1997). Nature of driving force for protein folding: A result from analyzing the statistical potential. Phys. Rev. Lett. 79, 765-768.
    • (1997) Phys. Rev. Lett. , vol.79 , pp. 765-768
    • Li, H.1    Tang, C.2    Wingreen, N.S.3
  • 29
    • 0029919190 scopus 로고    scopus 로고
    • Residue - residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading
    • Miyazawa, S. & Jernigan, R.L. (1996). Residue - residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading. J. Mol. Biol. 256, 623-644.
    • (1996) J. Mol. Biol. , vol.256 , pp. 623-644
    • Miyazawa, S.1    Jernigan, R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.