Linked Life Data

1569037

Source:http://linkedlifedata.com/resource/pubmed/id/1569037

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-5-27
pubmed:abstractText
The crystal structure of a calcium binding equine lysozyme has been determined at 2.5 A resolution by means of molecular replacement. The energy minimized equine lysozyme as the starting model, was refined with the molecular dynamics program, X-PLOR, and the R factor of the current model was found to be 24% without any water molecules. The conformation of the calcium binding loop is similar to that of alpha-lactalbumin. The profiles of backbone atomic displacements throughout the lysozyme and alpha-lactalbumin superfamilies are comparable as well as their homologous tertiary structures.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
111
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
141-3
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Crystallographic studies of a calcium binding lysozyme from equine milk at 2.5 A resolution.
pubmed:affiliation
Life Science Research Laboratory, Japan Tobacco, Inc., Kanagawa.
pubmed:publicationType
Journal Article