A search for the most stable folds of protein chains

It is generally believed that it is not sensible to search for a thermodynamically stable structure of a protein because neither a molecule nor a computer can look through all the 3(100) possible (for 100 residues) chain conformations. Here we show that the use of a molecular field theory for the lo...

Full description

Saved in:
Bibliographic Details
Published in:Nature (London) 1991-06, Vol.351 (6326), p.497-499
Main Authors: Finkelstein, Alexei V, Reva, Boris A
Format: Article
Language:English
Subjects:
algorithms
Biochemistry
Biological and medical sciences
Chemical Phenomena
Chemistry, Physical
conformation
Crystallins - chemistry
Fundamental and applied biological sciences. Psychology
General aspects
Mathematics
Mathematics in biology. Statistical analysis. Models. Metrology. Data processing in biology (general aspects)
Protein Conformation
Proteins
Proteins - chemistry
stability
Thermodynamics
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:It is generally believed that it is not sensible to search for a thermodynamically stable structure of a protein because neither a molecule nor a computer can look through all the 3(100) possible (for 100 residues) chain conformations. Here we show that the use of a molecular field theory for the long-range interactions, the use of one-dimensional statistical mechanics for the short-range ones and the discovery that there are and there must be only a small discrete set of folding patterns, make it possible to examine all the variety of 'potentially stable' structures. The general approach and its application is demonstrated here by calculation of stable folds for some beta domains. The most stable of these folds correspond to the observed structures.
ISSN:0028-0836
1476-4687
DOI:10.1038/351497a0