Linked Life Data

6378263

Source:http://linkedlifedata.com/resource/pubmed/id/6378263

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1984-9-19
pubmed:abstractText
High-resolution 1H-NMR spectroscopy at 600 MHz has been used to investigate the conformational transitions of the histidine-binding protein J of Salmonella typhimurium in solution as a function of pH and of L-histidine concentration. The dissociation constant for the binding of L-histidine to histidine-binding protein J increases from 6.0 X 10(-8) to 5.1 X 10(-7) M in going from pH 5.57 to 8.00. The conformation of this protein as observed by 1H-NMR also changes over this range of pH. However, when L-histidine is bound, the changes in conformation with pH are much smaller. Also, the pK for the single histidyl residue in histidine-binding protein J changes from 6.75 in the absence of L-histidine to 6.52 when L-histidine is bound. Earlier work in this laboratory resulted in the identification of several proton resonances believed to be at or near the L-histidine-binding site. Two of these resonances have been assigned to a tyrosine and the single histidyl residue in the histidine-binding protein J molecule.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0301-4622
pubmed:author
pubmed:issnType
Print
pubmed:volume
19
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
279-87
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
A high-resolution 1H-NMR investigation of the histidine-binding protein J of Salmonella typhimurium. Substrate-induced conformational changes.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.