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PMID: 8346235 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Engineering of stable and fast-folding sequences of model proteins.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 90 ·No. 15 ·1993-08-01 ·Pages 7195-9

Shakhnovich EI, Gutin AM

Abstract

The statistical mechanics of protein folding implies that the best-folding proteins are those that have the native conformation as a pronounced energy minimum. We show that this can be obtained by proper selection of protein sequences and suggest a simple practical way to find these sequences. The statistical mechanics of these proteins with optimized native structure is discussed. These concepts are tested with a simple lattice model of a protein with full enumeration of compact conformations. Selected sequences are shown to have a native state that is very stable and kinetically accessible.

MeSH Terms

Kinetics Models, Theoretical Protein Conformation Protein Engineering Proteins/chemistry Thermodynamics

Chemicals

Proteins

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Shakhnovich E I

Department of Chemistry, Harvard University, Cambridge, MA 02138.

Gutin A M

References (11)

11 references, click to expand

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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.90.15.7195

Published

1993-08-01

Pages

7195-9

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC47103

Subset

External Links

PubMed source DOI: 10.1073/pnas.90.15.7195 PMC Full Text View journal details

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