Linked Life Data

21361324

Source:http://linkedlifedata.com/resource/pubmed/id/21361324

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2011-3-17
pubmed:abstractText
Although previous experimental studies have shown the positional preference of different amino acids (AAs) to form a stable triple helical collagen motif, the structural basis for the variations in the sequence and the positional propensity has not been systematically investigated. Thus, we have here probed the origin of the structural stability offered by the 20 naturally occurring AAs to collagen by means of classical molecular dynamics (MD) simulation. Simulations were carried out on 39 collagen-like peptides employing a host-guest approach. The results show that the propensity of the different AAs to adopt collagen-like conformations depends primarily on their ? and ? angle preferences. Changes in these angles upon substitution of different AAs in the X(AA) and Y(AA) positions in the canonical ((Gly-X(AA)-Y(AA))(7))(3) motif dictate the formation of interchain hydrogen bonds, solvent interactions, and puckering of neighboring imino acids and, thus, the structural stability of the collagen. The role of solvent-mediated hydrogen bonds in the stabilization of collagen has also been elucidated from the MD simulations. In addition to the conventional hydrogen bonds known to be present in collagen, a hitherto unidentified direct interchain hydrogen bond, between the X(AA) N-H group and the Hyp O-H group of the neighboring chain, was observed during the simulations. Its occupancy was ?36% when Leu was present at the X(AA) position.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1520-5207
pubmed:author
pubmed:copyrightInfo
© 2011 American Chemical Society
pubmed:issnType
Electronic
pubmed:day
24
pubmed:volume
115
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2593-607
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Structural basis for the varying propensities of different amino acids to adopt the collagen conformation.
pubmed:affiliation
Chemical Laboratory, Central Leather Research Institute, Council of Scientific and Industrial Research, Adyar, Chennai 600 020, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't