Linked Life Data

7260038

Source:http://linkedlifedata.com/resource/pubmed/id/7260038

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1981-10-29
pubmed:abstractText
The pH dependence of the N-terminal 51 amino acid headpiece (HP) of the lac repressor has been followed by using 1H NMR spectroscopy to monitor the chemical shifts of resolved aromatic and methyl resonances. The NMR evidence reveals the folded HP domain to be stable from pH 1 to 10 at 23 degrees C. All observed resonances shift toward their expected random-coil positions above pH 10, which suggests that a general unfolding occurs. The four tyrosine rings reflect a combination of unfolding and titration in the order 7 greater than 17, 12 greater than 47. This pH-induced unfolding is completely reversible. In addition, strikingly similar pH behavior for selected tyrosine and methyl resonances at acid pH values suggests that clusters of various tyrosine, methyl, and carboxyl side chains exist in the native structure.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3346-50
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
pH dependence of the high-resolution proton nuclear magnetic resonance spectrum of the lac repressor headpiece.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.