Linked Life Data

11262940

Source:http://linkedlifedata.com/resource/pubmed/id/11262940

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2001-3-23
pubmed:abstractText
New computational models of the kinetics of natural site substitutions in proteins are described based on the underlying physical chemical properties of the amino acids. The corresponding reduction in the number of adjustable parameters allows us to analyze site-heterogeneity. Applying this evolutionary model to various data sets allows us to identify the important factors constraining molecular evolution, providing insight into the relationship between amino acid properties and protein structure.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1793-5091
pubmed:author
pubmed:issnType
Print
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
191-202
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Analyzing site heterogeneity during protein evolution.
pubmed:affiliation
Biophysics Research Division, University of Michigan, Ann Arbor, MI 48109-1055, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.