Optimal local propensities for model proteins
- 1 August 1995
- journal article
- research article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 22 (4) , 413-418
- https://doi.org/10.1002/prot.340220411
Abstract
Lattice models of proteins were used to examine the role of local propensities in stabilizing the native state of a protein, using techniques drawn from spin‐glass theory to characterize the free‐energy landscapes. In thestrongevolutionary limit, optimal conditions for folding are achieved when the contributions from local interactions to the stability of the native state is small. Further increasing the local interactions rapidly decreases the foldability.Keywords
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