Linked Life Data

9050158

Source:http://linkedlifedata.com/resource/pubmed/id/9050158

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-6-13
pubmed:abstractText
Rotational-echo, double-resonance (REDOR) NMR measurements of 31P-15N dipolar couplings have been made on a complex of Mg guanosine diphosphate (MgGDP) with uniformly 15N-labeled elongation factor Tu. The complex was embedded in a lyophilized buffer glass. The observed 15N REDOR dephasing by 31P was accounted for quantitatively by distances from 15N of Gly23 and Lys24 to P alpha and P beta of MgGDP as determined by X-ray crystallography of MgGDP complex formed using an elongation factor Tu that is missing a 15 residue loop in the vicinity of the binding site.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0926-2040
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
203-10
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Structural constraints on the complex of elongation factor Tu with magnesium guanosine diphosphate from rotational-echo double-resonance NMR.
pubmed:affiliation
Department of Chemistry, Washington University, St. Louis, MO 63130, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.