Linked Life Data

18345665

Source:http://linkedlifedata.com/resource/pubmed/id/18345665

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
2008-4-2
pubmed:abstractText
An isolated beta-sheet model system is investigated in a molecular beam experiment by means of mass- and isomer-selective IR/R2PI double resonance spectroscopy as well as ab initio and DFT calculations. As the exclusive intermolecular assembly, a beta-sheet motif is formed by spontaneous dimerization of two isolated peptide molecules. This secondary structure is produced from the tripeptide model Ac-Val-Tyr(Me)-NHMe without any further environment to form the binding motif which is analyzed by both the characteristic amide A and I vibrations. The experimental and theoretical investigations yield the assignment to an antiparallel beta-sheet model. The result of this detailed spectroscopic analysis on an isolated beta-sheet model indicates that there are intrinsic properties of a beta-sheet structure which can be formed without a solvent or a peptidic environment.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1520-5126
pubmed:author
pubmed:issnType
Electronic
pubmed:day
9
pubmed:volume
130
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4692-8
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Investigation of secondary structure elements by IR/UV double resonance spectroscopy: analysis of an isolated beta-sheet model system.
pubmed:affiliation
Heinrich-Heine Universität Düsseldorf, Institut für Physikalische Chemie I, Universitätsstrasse 26.33.O2, 40225 Düsseldorf, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't