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PMID: 7549881 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Domains in folding of model proteins.

Protein science : a publication of the Protein Society ·Vol. 4 ·No. 6 ·1995-06-00 ·Pages 1167-77

Abkevich VI, Gutin AM, Shakhnovich EI

Abstract

By means of Monte Carlo simulation, we investigated the equilibrium between folded and unfolded states of lattice model proteins. The amino acid sequences were designed to have pronounced energy minimum target conformations of different length and shape. For short fully compact (36-mer) proteins, the all-or-none transition from the unfolded state to the native state was observed. This was not always the case for longer proteins. Among 12 designed sequences with the native structure of a fully compact 48-mer, a simple all-or-none transition was observed in only three cases. For the other nine sequences, three states of behavior-the native, denatured, and intermediate states-were found. The contiguous part of the native structure (domain) was conserved in the intermediate state, whereas the remaining part was completely unfolded and structureless. These parts melted separately from each other.

MeSH Terms
Amino Acid Sequence Computer Simulation Models, Chemical Models, Molecular Molecular Sequence Data Monte Carlo Method Protein Conformation Protein Folding Proteins/chemistry Temperature
Chemicals
Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Abkevich V I
Department of Chemistry, Harvard University, Cambridge, Massachusetts 02138, USA.
Gutin A M
Shakhnovich E I
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21 references, click to expand
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Article Info
Journal
Protein science : a publication of the Protein Society
Abbr.
Protein Sci
ISSN
0961-8368
DOI
10.1002/pro.5560040615
Published
1995-06-00
Pages
1167-77
Language
English
Region
United States
NLM ID
9211750
PMCID
PMC2143143
Subset
IM
External Links
PubMed source DOI: 10.1002/pro.5560040615 PMC Full Text View journal details
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