Linked Life Data

16242834

Source:http://linkedlifedata.com/resource/pubmed/id/16242834

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2006-1-20
pubmed:abstractText
The replacement of hydrogen with deuterium is frequently used in conjunction with neutron diffraction to investigate peptide-membrane interaction. This isotopic substitution in an amino acid residue radically changes the neutron scatter pattern of the peptide, thereby allowing its localisation within the bilayer with the aid of derived Fourier maps. Nonetheless, this technique relies on the generally held assumption that normal and isotopically enriched protein species do not differ significantly in structure or biological activity. Recently, this assumption has been questioned and here, diffraction data from studies on a membrane interactive peptide clearly challenge the reliability of this assumption.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0301-4622
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
119
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
115-20
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Deuteration can affect the conformational behaviour of amphiphilic alpha-helical structures.
pubmed:affiliation
Faculty of Science, University of Central Lancashire, Preston, PR1 2HE, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't