DOI: 10.1016/s1359-0278(96)00033-8. Improved design of stable and fast-folding model proteins

Improved design of stable and fast-folding model proteins

10.1016/s1359-0278(96)00033-8

Crossref journal-article

Elsevier BV

Folding and Design (78)

Bibliography

Abkevich, V. I., Gutin, A. M., & Shakhnovich, E. I. (1996). Improved design of stable and fast-folding model proteins. Folding and Design, 1(3), 221â230.

Authors 3

Victor I Abkevich (first)
Alexander M Gutin (additional)
Eugene I Shakhnovich (additional)

References 36 Referenced 66

10.1073/pnas.89.11.4918 / Proc. Natl. Acad. Sci. USA / Optimal protein-folding codes from spin-glass theory by Goldstein (1992)
10.1073/pnas.90.15.7195 / Proc. Natl. Acad. Sci. USA / Engineering of stable and fast-folding sequences of model proteins by Shakhnovich (1993)
10.1006/jmbi.1994.1110 / J. Mol. Biol / Kinetics of protein folding: a lattice model study for the requirements for folding to the native state by Sali (1994)
10.1103/PhysRevLett.72.3907 / Phys. Rev. Lett / Proteins with selected sequences fold to their unique native conformation by Shakhnovich (1994)
10.1063/1.468920 / J. Chem. Phys / Statistical thermodynamics of protein folding: comparison of a mean-field theory with Monte-Carlo simulations by Hao (1995)
10.1073/pnas.92.5.1282 / Proc. Natl. Acad. Sci. USA / Evolution-like selection of fast-folding model proteins by Gutin (1995)
10.1126/science.1853201 / Science / A method to identify protein sequences that fold into a known three-dimensional structure by Bowie (1991)
10.1093/protein/6.8.793 / Protein Eng / A novel approach to design of stable proteins by Shakhnovich (1993)
10.1006/jmbi.1995.0511 / J. Mol. Biol / Impact of local and non-local interactions on thermodynamics and kinetics of protein folding by Abkevich (1995)
10.1103/PhysRevLett.76.323 / Phys. Rev. Lett / New algorithm for protein design by Deutch (1996)
10.1016/S1359-0278(96)00019-3 / Folding & Design / Universality and diversity of the protein folding scenarios: a comprehensive analysis with the aid of lattice model by Mirny (1996)
10.1002/pro.5560040615 / Protein Sci / Domains in folding of model proteins by Abkevich (1995)
10.1016/S0065-3233(08)60460-X / Adv. Protein Chem / Stability of proteins. Small single-domain proteins by Privalov (1979)
10.1016/S0065-3233(08)60468-4 / Adv. Protein Chem / Stability of proteins: proteins which do not present a single cooperative system by Privalov (1982)
10.1021/bi00201a035 / Biochemistry / Three-state thermodynamic analysis of the denaturation of staphylococcal nuclease mutants by Carra (1994)
10.1038/349633a0 / Nature / Demonstration by NMR of folding domains in lysozyme by Miranker (1991)
10.1063/1.467320 / J. Chem. Phys / Free energy landscape for protein folding kinetics. Intermediates, traps and multiple pathways in theory and lattice model simulations by Abkevich (1994)
10.1063/1.466677 / J. Chem. Phys / Transition states and folding dynamics of proteins and heteropolymers by Chan (1994)
10.1002/bip.360350114 / Biopolymers / Nucleation mechanism for protein folding and theoretical predictions for hydrogen-exchange labelling experiments by Thirumalai (1995)
10.1002/prot.340210302 / Proteins / Funnels, pathways, and the energy landscape of protein folding: a synthesis by Bryngelson (1995)
10.1073/pnas.92.20.9029 / Proc. Natl. Acad. Sci. USA / Kinetic traps in lysozyme folding by Kiefhaber (1995)
10.1021/ma00145a039 / Macromolecules / Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximation, Table VI by Miyazawa (1985)
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10.1063/1.1679979 / J. Chem. Phys / Monte Carlo studies of lattice model polymer chains. III. Relaxation of Rouse coordinates by Verdier (1973)
10.1063/1.431297 / J. Chem. Phys / Analysis of monte-carlo results on the kinetics of lattice polymer chains with excluded volume by Hilhorst (1975)
10.1063/1.1699114 / J. Chem. Phys / Equation of state calculations by fast computing machines by Metropolis (1953)
10.1111/j.1399-3011.1975.tb02465.x / Int. J. Peptide Protein Res / Studies on protein folding, unfolding and fluctuations by computer simulation by Taketomi (1975)
10.1021/bi00009a038 / Biochemistry / Is burst hydrophobic collapse necessary for rapid folding? by Gutin (1995)
10.1038/369248a0 / Nature / How does a protein fold? by Sali (1994)
10.1103/PhysRevLett.63.1195 / Phys. Rev. Lett / Optimized monte carlo data analysis by Ferrenberg (1989)
10.1063/1.470610 / J. Chem. Phys / Kinetics and thermodynamic analysis of protein-like heteropolymer: Monte Carlo histogram technique by Socci (1995)
10.1063/1.462462 / J. Chem. Phys / Folding kinetics of proteins and copolymers by Miller (1992)
10.1103/PhysRevB.24.2613 / Phys. Rev / Random energy model: an exactly solvable model of disordered systems by Derrida (1981)
10.1073/pnas.84.21.7524 / Proc. Natl. Acad. Sci. USA / Spin glasses and the statistical mechanics of protein folding by Bryngelson (1987)
10.1209/0295-5075/9/6/013 / Europhys. Lett / Relaxation to equilibrium in the random energy model by Shakhnovich (1989)
10.1016/0301-4622(89)80058-4 / Biophys. Chem / Formation of unique structure in polypeptide chains. Theoretical investigation with the aid of a replica approach by Shakhnovich (1989)

Dates

Type	When
Created	20 years, 1 month ago (July 7, 2005, 11:24 a.m.)
Deposited	6 years, 7 months ago (Jan. 24, 2019, 12:51 p.m.)
Indexed	1 year ago (Aug. 4, 2024, 7:22 a.m.)
Issued	29 years, 3 months ago (June 1, 1996)
Published	29 years, 3 months ago (June 1, 1996)
Published Print	29 years, 3 months ago (June 1, 1996)

Funders 0

None

BibTeX

@article{Abkevich_1996, title={Improved design of stable and fast-folding model proteins}, volume={1}, ISSN={1359-0278}, url={http://dx.doi.org/10.1016/s1359-0278(96)00033-8}, DOI={10.1016/s1359-0278(96)00033-8}, number={3}, journal={Folding and Design}, publisher={Elsevier BV}, author={Abkevich, Victor I and Gutin, Alexander M and Shakhnovich, Eugene I}, year={1996}, month=jun, pages={221–230} }

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