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Optimal local propensities for model proteins
Author(s) -
Govindarajan Sridhar,
Goldstein Richard A.
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340220411
Subject(s) - statistical physics , limit (mathematics) , native state , energy landscape , protein folding , stability (learning theory) , folding (dsp implementation) , spin glass , lattice protein , state (computer science) , physics , evolutionary biology , computer science , mathematics , biology , condensed matter physics , engineering , thermodynamics , algorithm , mathematical analysis , nuclear magnetic resonance , machine learning , electrical engineering
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 the strong evolutionary 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. © 1995 Wiley‐Liss, Inc.