Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1982-9-10
pubmed:abstractText
4-(Trifluoromethyl)-alpha-bromoacetanilide is structurally similar to a large number of compounds that inactivate alpha-chymotrypsin by alkylating the methionine-192 residue or occasionally serine-195. Fluorine nuclear magnetic resonance (NMR) experiments suggest that this material reacts with the enzyme at two distinct loci. One of these involves alkylation of methionine while reaction at a second site, which does not appear to be near the active site, diminishes the proclivity for reaction at methionine. Solvent effects (H2O/D2O) and fluorine-proton Overhauser experiments indicate that the reporter group attached to methionine closely contacts the protein surface and is thereby shielded from solvent while the CF3 group at the second site is more accessible to solvent.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2299-304
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Reactions of alpha-chymotrypsin with 4-(trifluoromethyl)-alpha-bromoacetanilide.
pubmed:publicationType
Journal Article, Comparative Study, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.