Linked Life Data

9084681

Source:http://linkedlifedata.com/resource/pubmed/id/9084681

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-4
pubmed:dateCreated
1997-5-15
pubmed:abstractText
The crystal structure of the collagen-based peptide (Pro-Hyp-Gly)4-Pro-Hyp-Ala-(Pro-Hyp-Gly)5 has provided for the first time a highly detailed picture of the architectural elements that come into play in the collagen triple helix. The center of the molecule, which harbors a Gly-->Ala substitution, shows subtle conformational changes that result in a local untwisting of the triple helix. The characteristic hydrogen bonding pattern of collagen triple helices is replaced by interstitial water bridges. These effects may be relevant to the diseased states derived from Gly-->X mutations in collagens. The possible implications of this disrupted architecture for collagen assemblies are discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-8207
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
401-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Disrupted collagen architecture in the crystal structure of a triple-helical peptide with a Gly-->Ala substitution.
pubmed:affiliation
Department of Chemistry, Rutgers University, Piscataway, NJ 08855, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't