메뉴 건너뛰기




Volumn 86, Issue 5, 2004, Pages 2758-2764

Stability and the Evolvability of Function in a Model Protein

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND;

EID: 1842835981     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(04)74329-5     Document Type: Article
Times cited : (87)

References (37)
  • 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
    • 0032478172 scopus 로고    scopus 로고
    • Enzyme engineering reaches the boiling point
    • Amold, F. H. 1998. Enzyme engineering reaches the boiling point. Proc. Natl. Acad. Sci. USA. 95:2035-2036.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2035-2036
    • Amold, F.H.1
  • 4
    • 0033533517 scopus 로고    scopus 로고
    • Neutral evolution of model proteins: Diffusion in sequence space and overdispersion
    • Bastolla, U., H. E. Roman, and M. Vendruscolo. 1999. Neutral evolution of model proteins: diffusion in sequence space and overdispersion. J. Theor. Biol. 200:49-64.
    • (1999) J. Theor. Biol. , vol.200 , pp. 49-64
    • Bastolla, U.1    Roman, H.E.2    Vendruscolo, M.3
  • 5
    • 0000105754 scopus 로고    scopus 로고
    • Structurally constrained protein evolution: Results from a lattice simulation
    • Bastolla, U., M. Vendruscolo, and H. E. Roman. 2000. Structurally constrained protein evolution: results from a lattice simulation. Eur. Phys. J. B. 15:385-397.
    • (2000) Eur. Phys. J. B , vol.15 , pp. 385-397
    • Bastolla, U.1    Vendruscolo, M.2    Roman, H.E.3
  • 6
    • 13044269058 scopus 로고    scopus 로고
    • Modeling evolutionary landscapes: Mutational stability, topology, and superfunnels in sequence space
    • Bornberg-Bauer, E., and H. S. Chan. 1999. Modeling evolutionary landscapes: mutational stability, topology, and superfunnels in sequence space. Proc. Natl. Acad. Sci. USA. 96:10689-10694.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10689-10694
    • Bornberg-Bauer, E.1    Chan, H.S.2
  • 8
    • 0013527261 scopus 로고    scopus 로고
    • Perspectives on protein evolution from simple exact models
    • Chan, H. S., and E. Bornberg-Bauer. 2002. Perspectives on protein evolution from simple exact models. Applied Bioinformatics. 1:121-144.
    • (2002) Applied Bioinformatics , vol.1 , pp. 121-144
    • Chan, H.S.1    Bornberg-Bauer, E.2
  • 9
    • 0037154157 scopus 로고    scopus 로고
    • Recombinatoric exploration of novel folded structures: A heteropolymer-based model of protein evolutionary landscapes
    • Cui, Y., W. H. Wong, E. Bornberg-Bauer, and H. S. Chan. 2002. Recombinatoric exploration of novel folded structures: a heteropolymer-based model of protein evolutionary landscapes. Proc. Natl. Acad. Sci. USA. 99:809-814.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 809-814
    • Cui, Y.1    Wong, W.H.2    Bornberg-Bauer, E.3    Chan, H.S.4
  • 10
    • 0029120253 scopus 로고
    • Cooperatively folded proteins in random sequence libraries
    • Davidson, A. R., K. J. Lumb, and R. T. Sauer. 1995. Cooperatively folded proteins in random sequence libraries. Nat. Struct. Biol. 2:856-864.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 856-864
    • Davidson, A.R.1    Lumb, K.J.2    Sauer, R.T.3
  • 15
    • 0028149160 scopus 로고
    • Exploring conformational space with a simple lattice model for protein-structure
    • Hinds, D. A., and M. Levitt. 1994. Exploring conformational space with a simple lattice model for protein-structure. J. Mol. Biol. 243:668-682.
    • (1994) J. Mol. Biol. , vol.243 , pp. 668-682
    • Hinds, D.A.1    Levitt, M.2
  • 16
    • 0032864055 scopus 로고    scopus 로고
    • The evolutionary landscape of functional model proteins
    • Hirst, J. D. 1999. The evolutionary landscape of functional model proteins. Protein Eng. 12721-726.
    • (1999) Protein Eng. , pp. 12721-12726
    • Hirst, J.D.1
  • 17
    • 0035810165 scopus 로고    scopus 로고
    • Functional proteins from a random-sequence library
    • Keefe, A. D., and J. W. Szostak. 2001. Functional proteins from a random-sequence library. Nature. 410:715-718.
    • (2001) Nature , vol.410 , pp. 715-718
    • Keefe, A.D.1    Szostak, J.W.2
  • 18
    • 0037022286 scopus 로고    scopus 로고
    • Protein topology and stability define the space of allowed sequences
    • Koehl, P., and M. Levitt. 2002. Protein topology and stability define the space of allowed sequences. Proc. Natl. Acad. Sci. USA. 993:1280-1285.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.993 , pp. 1280-1285
    • Koehl, P.1    Levitt, M.2
  • 19
    • 0030867610 scopus 로고    scopus 로고
    • Ligand binding to proteins: The binding landscape model
    • Miller, D. W., and K. A. Dill. 1997. Ligand binding to proteins: the binding landscape model. Protein Sci. 6:2166-2179.
    • (1997) Protein Sci. , vol.6 , pp. 2166-2179
    • Miller, D.W.1    Dill, K.A.2
  • 21
    • 33845377127 scopus 로고
    • Estimation of effective interresidue contact energies from protein crystal structures: Quasi-chemical approximation
    • Miyazawa, S., and R. L. Jernigan. 1985. Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximation. Macromolecules. 18:534-552.
    • (1985) Macromolecules , vol.18 , pp. 534-552
    • Miyazawa, S.1    Jernigan, R.L.2
  • 22
    • 0000868685 scopus 로고    scopus 로고
    • Are two distributions different?
    • in C. Cambridge University Press, Cambridge, UK
    • Press, W. H., S. A. Teukolsky, W. T. Vetterling, and B. P. Flannery, editors 2002. Are two distributions different? In Numerical Recipes in C. Cambridge University Press, Cambridge, UK. 620-628.
    • (2002) Numerical Recipes , pp. 620-628
    • Press, W.H.1    Teukolsky, S.A.2    Vetterling, W.T.3    Flannery, B.P.4
  • 23
    • 0023456254 scopus 로고
    • Algorithms for lattice statistics
    • Rapaport, D. C. 1987. Algorithms for lattice statistics. Comput. Phys. Rep. 5:265-350.
    • (1987) Comput. Phys. Rep. , vol.5 , pp. 265-350
    • Rapaport, D.C.1
  • 24
    • 0029644328 scopus 로고
    • Hyperthermophiles: Taking the heat and loving it
    • Rees, D. C., and M. W. W. Adams. 1995. Hyperthermophiles: taking the heat and loving it. Structure. 3:251-254.
    • (1995) Structure , vol.3 , pp. 251-254
    • Rees, D.C.1    Adams, M.W.W.2
  • 25
    • 0028774340 scopus 로고
    • Stability and function: Two constraints in the evolution of barstar and other proteins
    • Schreiber, G., A. M. Buckle, and A. R. Fersht. 1994. Stability and function: two constraints in the evolution of barstar and other proteins. Structure. 2:945-951.
    • (1994) Structure , vol.2 , pp. 945-951
    • Schreiber, G.1    Buckle, A.M.2    Fersht, A.R.3
  • 26
    • 0027441807 scopus 로고
    • Step-wise mutation of barnase to binase: A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability
    • Serrano, L., A. G. Day, and A. R. Fersht. 1993. Step-wise mutation of barnase to binase: a procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. J. Mol. Biol. 233:305-312.
    • (1993) J. Mol. Biol. , vol.233 , pp. 305-312
    • Serrano, L.1    Day, A.G.2    Fersht, A.R.3
  • 27
    • 0031745665 scopus 로고    scopus 로고
    • Protein design: A perspective from simple tractable models
    • Shakhnovich, E. I. 1998. Protein design: a perspective from simple tractable models. Fold. Des. 3:R45-R58.
    • (1998) Fold. Des. , vol.3
    • Shakhnovich, E.I.1
  • 28
    • 0027234766 scopus 로고
    • Engineering of stable and fast-folding sequences of model proteins
    • Shakhnovich, E. I., and A. M. Gutin. 1993. Engineering of stable and 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
  • 30
    • 0032147243 scopus 로고    scopus 로고
    • Protein folding mechanisms and the multidimensional folding funnel
    • Socci, N. D., J. N. Onuchic, and P. G. Wolynes. 1998. Protein folding mechanisms and the multidimensional folding funnel. Proteins. 32:136-158.
    • (1998) Proteins , vol.32 , pp. 136-158
    • Socci, N.D.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 31
    • 0028949615 scopus 로고
    • Proteins and temperature
    • Somero, G. N. 1995. Proteins and temperature. Annu. Rev. Physiol. 57:43-68.
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 43-68
    • Somero, G.N.1
  • 32
    • 0033987966 scopus 로고    scopus 로고
    • The distribution of structures in evolving protein populations
    • Taverna, D. M., and R. A. Goldstein. 2000. The distribution of structures in evolving protein populations. Biopolymers. 53:1-8.
    • (2000) Biopolymers , vol.53 , pp. 1-8
    • Taverna, D.M.1    Goldstein, R.A.2
  • 33
    • 0036139093 scopus 로고    scopus 로고
    • Why are proteins marginally stable?
    • Taverna, D. M., and R. A. Goldstein. 2002. Why are proteins marginally stable? Proteins. 46:105-109.
    • (2002) Proteins , vol.46 , pp. 105-109
    • Taverna, D.M.1    Goldstein, R.A.2
  • 34
    • 0034656952 scopus 로고    scopus 로고
    • Hiking in the energy landscape in sequence space: A bumpy road to good folders
    • Tiana, G., R. Broglia, and E. Shakhnovich. 2000. Hiking in the energy landscape in sequence space: a bumpy road to good folders. Proteins. 39:244-251.
    • (2000) Proteins , vol.39 , pp. 244-251
    • Tiana, G.1    Broglia, R.2    Shakhnovich, E.3
  • 35
    • 0036295508 scopus 로고    scopus 로고
    • Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs
    • Wang, X., G. Minasov, and B. K. Shoichet. 2002. Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs. J. Mol. Biol. 320:85-95.
    • (2002) J. Mol. Biol. , vol.320 , pp. 85-95
    • Wang, X.1    Minasov, G.2    Shoichet, B.K.3
  • 37
    • 0036678845 scopus 로고    scopus 로고
    • Roles of mutation and recombination in the evolution of protein thermodynamics
    • Xia, Y., and M. Levitt. 2002. Roles of mutation and recombination in the evolution of protein thermodynamics. Proc. Natl. Acad. Sci. USA. 16:10382-10387.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.16 , pp. 10382-10387
    • Xia, Y.1    Levitt, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.