Linked Life Data

11373724

Source:http://linkedlifedata.com/resource/pubmed/id/11373724

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-5-24
pubmed:abstractText
beta-Helix structures are of particular interest due to their capacity to form transmembrane channels with different transport properties. However, the relatively large number of beta-helices configurations does not allow a direct conformational analysis of beta-helical oligopeptides. A synthetic alternating D,L-oligopeptide with twelve norleucines (XIIMe) has been used as a model to get insight in the conformational features of beta-helix structures. The spatial configuration of XIIMe in solution has been determined by NMR. An extensive set of distances (nuclear Overhauser effect) and dihedral (J coupling constants) constraints have been included in molecular dynamics calculations. The NMR experimental data and theoretical calculations clearly indicate that the XIIMe adopts a single beta(4.4)-helix-type conformation in nonpolar solvents.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-3525
pubmed:author
pubmed:copyrightInfo
Copyright 2001 John Wiley & Sons, Inc. Biopolymers 59: 110-119, 2001
pubmed:issnType
Print
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
110-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Solution NMR structure of a D,L-alternating oligonorleucine as a model of beta-helix.
pubmed:affiliation
Departamento de Química Física, Facultat de Químicas, Universitat de Valencia, C/Dr. Moliner, 50, 46100-Burjassot (Valencia), Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't