Designability and Thermal Stability of Protein Structures

Thumbnail Image

Date

Authors

Journal Title

Journal ISSN

Volume Title

Publisher

Abstract

Description

Only about 1,000 qualitatively different protein folds are believed to exist in nature. Here, we review theoretical studies which suggest that some folds are intrinsically more designable than others, {\it i.e.} are lowest energy states of an unusually large number of sequences. The sequences associated with these folds are also found to be unusually thermally stable. The connection between highly designable structures and highly stable sequences is generally known as the "designability principle". The designability principle may help explain the small number of natural folds, and may also guide the design of new folds.
12 pages, 10 figures, a review to be published in Polymer

Keywords

Statistical Mechanics, Soft Condensed Matter, Biological Physics, Biomolecules

Citation

URI

http://salesiana.dossiersoluciones.com/handle/123456789/21115

Consulte el texto completo en el siguiente enlace:

https://arxiv.org/abs/cond-mat/0303600
 http://arxiv.org/abs/cond-mat/0303600

Collections

arXiv