Linked Life Data

11370779

Source:http://linkedlifedata.com/resource/pubmed/id/11370779

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2001-5-23
pubmed:abstractText
Unravelling the factors that contribute to the formation and the stability of beta-sheet structure in peptides is a subject of great current interest. A beta-hairpin, the smallest beta-sheet motif, consists of two antiparallel hydrogen-bonded beta-strands linked by a loop region. We have performed a statistical analysis on protein beta-hairpins showing that the most abundant types of beta-hairpins, 2:2, 3:5 and 4:4, have characteristic patterns of 13C(alpha) and 13C(beta) conformational shifts, as expected on the basis of their phi and psi angles. This fact strongly supports the potential value of 13C(alpha) and 13C(beta) conformational shifts as a means to identify beta-hairpin motifs in peptides. Their usefulness was confirmed by analysing the patterns of 13C(alpha) and 13C(beta) conformational shifts in 13 short peptides, 10-15 residues long, that adopt beta-hairpin structures in aqueous solution. Furthermore, we have investigated their potential as a method to quantify beta-hairpin populations in peptides.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0925-2738
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
331-45
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
13C(alpha) and 13C(beta) chemical shifts as a tool to delineate beta-hairpin structures in peptides.
pubmed:affiliation
Instituto de Estructura de la Materia, Consejo Superior de Investigaciones Científicas, Madrid, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't