Linked Life Data

8338832

Source:http://linkedlifedata.com/resource/pubmed/id/8338832

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
29
pubmed:dateCreated
1993-8-31
pubmed:abstractText
Conformational energy computations have been used to demonstrate that side-chain-backbone interactions contribute substantially to the stabilization of the triple-helical structure of collagen with a natural sequence. The minimum-energy conformation has been determined for a short triple-helical segment from the N-terminus of type I bovine skin collagen, containing 12 residues in each strand. In this conformation, the side chains of three Arg and four Met residues fold tightly against the triple-helical backbone, forming numerous atomic contacts with the neighboring strand. In addition, the polar groups of the three Arg and two Ser residues form hydrogen bonds with backbone carbonyl groups. The estimated total stabilization due to the side-chain interactions is about -50 kcal/mol out of a total interchain energy of -193.5 kcal/mol. The study presented here is the first application of conformational energy computations to a real sequence in the collagen molecule.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7354-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Stabilization of the triple-helical structure of natural collagen by side-chain interactions.
pubmed:affiliation
Dipartimento di Chimica, Università di Napoli, Italy.
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