Literature DB >> 9408943

Evolution of model proteins on a foldability landscape.

S Govindarajan1, R A Goldstein.   

Abstract

We model the evolution of simple lattice proteins as a random walk in a fitness landscape, where the fitness represents the ability of the protein to fold. At higher selective pressure, the evolutionary trajectories are confined to neutral networks where the native structure is conserved and the dynamics are non self-averaging and nonexponential. The optimizability of the corresponding native structure has a strong effect on the size of these neutral networks and thus on the nature of the evolutionary process.

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Year:  1997        PMID: 9408943     DOI: 10.1002/(sici)1097-0134(199712)29:4<461::aid-prot6>3.0.co;2-b

Source DB:  PubMed          Journal:  Proteins        ISSN: 0887-3585


  29 in total

1.  Conformational propagation with prion-like characteristics in a simple model of protein folding.

Authors:  P M Harrison; H S Chan; S B Prusiner; F E Cohen
Journal:  Protein Sci       Date:  2001-04       Impact factor: 6.725

2.  Folding simulation of protein models on the structure-based cubo-octahedral lattice with the Contact Interactions algorithm.

Authors:  L Toma; S Toma
Journal:  Protein Sci       Date:  1999-01       Impact factor: 6.725

3.  On hydrophobicity correlations in protein chains.

Authors:  A Irbäck; E Sandelin
Journal:  Biophys J       Date:  2000-11       Impact factor: 4.033

4.  Evolution of functionality in lattice proteins.

Authors:  P D Williams; D D Pollock; R A Goldstein
Journal:  J Mol Graph Model       Date:  2001       Impact factor: 2.518

5.  Buffed energy landscapes: another solution to the kinetic paradoxes of protein folding.

Authors:  Steven S Plotkin; Peter G Wolynes
Journal:  Proc Natl Acad Sci U S A       Date:  2003-04-03       Impact factor: 11.205

6.  Roles of mutation and recombination in the evolution of protein thermodynamics.

Authors:  Yu Xia; Michael Levitt
Journal:  Proc Natl Acad Sci U S A       Date:  2002-07-29       Impact factor: 11.205

7.  Funnel-like organization in sequence space determines the distributions of protein stability and folding rate preferred by evolution.

Authors:  Yu Xia; Michael Levitt
Journal:  Proteins       Date:  2004-04-01

8.  Rapid evolution in conformational space: a study of loop regions in a ubiquitous GTP binding domain.

Authors:  Christian Blouin; Davin Butt; Andrew James Roger
Journal:  Protein Sci       Date:  2004-03       Impact factor: 6.725

9.  Evolvability and single-genotype fluctuation in phenotypic properties: a simple heteropolymer model.

Authors:  Tao Chen; David Vernazobres; Tetsuya Yomo; Erich Bornberg-Bauer; Hue Sun Chan
Journal:  Biophys J       Date:  2010-06-02       Impact factor: 4.033

10.  Comparing folding codes in simple heteropolymer models of protein evolutionary landscape: robustness of the superfunnel paradigm.

Authors:  Richard Wroe; Erich Bornberg-Bauer; Hue Sun Chan
Journal:  Biophys J       Date:  2004-10-22       Impact factor: 4.033

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