Linked Life Data

10550209

Source:http://linkedlifedata.com/resource/pubmed/id/10550209

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-11-19
pubmed:abstractText
This article is a personal perspective on the developments in the field of protein folding over approximately the last 40 years. In addition to its historical aspects, the article presents a view of the principles of protein folding with particular emphasis on the relationship of these principles to the problem of protein structure prediction. It is argued that despite much that is new, the essential elements of our current understanding of protein folding were anticipated by researchers many years ago. These elements include the recognition of the central importance of the polypeptide backbone as a determinant of protein conformation, hierarchical protein folding, and multiple folding pathways. Important areas of progress include a detailed characterization of the folding pathways of a number of proteins and a fundamental understanding of the physical chemical forces that determine protein stability. Despite these developments, fold prediction algorithms still encounter difficulties in identifying the correct fold for a given sequence. This may be due to the possibility that the free energy differences between at least a few alternate conformations of many proteins are not large. Significant progress in protein structure prediction has been due primarily to the explosive growth of sequence and structural databases. However, further progress is likely to depend in part on the ability to combine information available from databases with principles and algorithms derived from physical chemical studies of protein folding. An approach to the integration of the two areas is outlined with specific reference to the PrISM program that is a fully integrated sequence/structural-analysis/fold-recognition/homology model building software system.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Academic Press.
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
293
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
283-93
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Protein folding: from the levinthal paradox to structure prediction.
pubmed:affiliation
Department of Biochemistry and Molecular Biophysics, Columbia University, 630 West 168 St., New York, NY 10032, USA. bh6@columbia.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Review