Why are proteins so robust to site mutations?
- 1 January 2002
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 315 (3), 479-484
- https://doi.org/10.1006/jmbi.2001.5226
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Evolution of functionality in lattice proteinsJournal of Molecular Graphics and Modelling, 2001
- Plasticity, evolvability, and modularity in RNAJournal of Experimental Zoology, 2000
- The distribution of structures in evolving protein populationsPeptide Science, 2000
- Modeling evolutionary landscapes: Mutational stability, topology, and superfunnels in sequence spaceProceedings of the National Academy of Sciences of the United States of America, 1999
- Neutral Evolution of Model Proteins: Diffusion in Sequence Space and OverdispersionJournal of Theoretical Biology, 1999
- De Novo Design and Structural Characterization of Proteins and MetalloproteinsAnnual Review of Biochemistry, 1999
- Use of propensities of amino acids to the local structural environments to understand effect of substitution mutations on protein stability.Protein Engineering, Design and Selection, 1998
- Continuity in Evolution: On the Nature of TransitionsScience, 1998
- The sequences of small proteins are not extensively optimized for rapid folding by natural selectionProceedings of the National Academy of Sciences of the United States of America, 1998
- The folding of an enzyme: II. Substructure of barnase and the contribution of different interactions to protein stabilityJournal of Molecular Biology, 1992