Linked Life Data

11761158

Source:http://linkedlifedata.com/resource/pubmed/id/11761158

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-12-11
pubmed:abstractText
The conformation of a model peptide (Ala-Lys-Pro-Ser-Tyr-Hyp-Hyp-Thr-Tyr-Lys) of the tandem repeat decapeptide sequence of Mytilus edulis foot protein-1 (mefp-1) has been studied by 1H and 13C 2D-NMR in three diverse media-DMSO-d6, water (pH 3.5) and 40% hexafluoroacetone (HFA). Various NMR parameters that were used to deduce the secondary structure were chemical shift (1H and 13C) temperature coefficients of NH chemical shifts, 3J(NH alpha) coupling constants and the pattern of intra and inter-residue NOEs. Molecular dynamics simulations making integral use of the NMR data shows that the conformation of the peptide is conserved in all the three media. The structure in the three solvents is best defined as a left-handed polyproline II helix (PPII).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0142-9612
pubmed:author
pubmed:issnType
Print
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
389-96
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Conformation of a model peptide of the tandem repeat decapeptide in mussel adhesive protein by NMR and MD simulations.
pubmed:affiliation
Department of Pharmaceutical Chemistry, Bombay College of Pharmacy, Kalina, Mumbai, India
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't