Linked Life Data

15772755

Source:http://linkedlifedata.com/resource/pubmed/id/15772755

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2005-3-17
pubmed:abstractText
Nitroxide species, which have an unpaired electron localized on a nitrogen atom, can be useful as NMR probes to identify areas of the surface of a protein involved in the formation of a complex. The proximity of an electron spin leads to higher NMR relaxation rates for protein nuclei. If a protein-ligand complex is formed the radical is excluded from certain sites on the protein surface, protecting them from relaxation effects. We show here that charged nitroxide species can be helpful for identifying regions of the surface of the 4F1(5)F1 module pair from human fibronectin involved in peptide binding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0925-2738
pubmed:author
pubmed:issnType
Print
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
155-60
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Probing protein-peptide binding surfaces using charged stable free radicals and transverse paramagnetic relaxation enhancement (PRE).
pubmed:affiliation
Department of Biochemistry, University of Oxford, South Parks Road, OX1 3QU, Oxford, UK. Michael.Deschamps@bioch.ox.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't