Linked Life Data

1517010

Source:http://linkedlifedata.com/resource/pubmed/id/1517010

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-10-7
pubmed:abstractText
The NMR spectra of the Leu48----Ala mutant of human transforming growth factor alpha were compared to that of the wild-type. All chemical shift changes are less than or equal to 0.02 ppm with the exception of resonances associated with residues 47, 48 and 50 (all less than or equal to 0.07 ppm). Minimal changes were observed for NOEs associated with residues Val1 to His45. The weakening of some NOEs associated with the region Ala46-Ala50 may suggest a slightly increased flexibility for this region. Refinement of the previously calculated wild-type structures using distance constraints derived from the L48A mutant had little overall effect. Leu48-Ala50 is ill-defined for both wild-type and mutant proteins. These results suggest that Leu48 has no structural role and thus must be an important factor in the protein-receptor interface.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0367-8377
pubmed:author
pubmed:issnType
Print
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
111-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
NMR study on solution structure of the site-specific mutant Leu48----Ala transforming growth factor alpha.
pubmed:affiliation
SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.