Funnel-like organization in sequence space determines the distributions of protein stability and folding rate preferred by evolution
- 5 February 2004
- journal article
- research article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 55 (1) , 107-114
- https://doi.org/10.1002/prot.10563
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Why are proteins so robust to site mutations?Journal of Molecular Biology, 2002
- Why are proteins marginally stable?Proteins-Structure Function and Bioinformatics, 2001
- The distribution of structures in evolving protein populationsBiopolymers, 2000
- Shaping Space: the Possible and the Attainable in RNA Genotype–phenotype MappingJournal of Theoretical Biology, 1998
- Impact of Local and Non-local Interactions on Thermodynamics and Kinetics of Protein FoldingJournal of Molecular Biology, 1995
- Principles of protein folding — A perspective from simple exact modelsProtein Science, 1995
- How does a protein fold?Nature, 1994
- The neutral theory of molecular evolution: A review of recent evidence.The Japanese Journal of Genetics, 1991
- Implications of thermodynamics of protein folding for evolution of primary sequencesNature, 1990
- Natural Selection and the Concept of a Protein SpaceNature, 1970