Protein stability and foldability–designability complementarity

We address the question of how evolution has possibly enhanced protein functionality by a complementary selection of sequences and structures. We show how the requirement of good functionality implies a two-way link between thermodynamic stability and resistance against mutations. The existence of families of structures emerges as a possible consequence of these evolution criteria.

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Year of publication:	1998
Authors:	Vendruscolo, Michele
Published in:	Physica A: Statistical Mechanics and its Applications. - Elsevier, ISSN 0378-4371. - Vol. 249.1998, 1, p. 576-580
Publisher:	Elsevier
Subject:	Protein folding \| Mutations \| Thermodynamic stability

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Type of publication:	Article
Source:	RePEc - Research Papers in Economics

Persistent link: https://www.econbiz.de/10010599437