Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1984-6-22
pubmed:abstractText
The circular dichroism spectrum of the catalytic subunit of cAMP-dependent protein kinase was measured in the far-UV (190-240 nm) and near-UV (250-300 nm) region. Data from the far-UV spectra were processed with the CONTIN program for estimation of globular protein secondary structure [ Provencher , S. W. (1982) CONTIN (Version 2) User's Manual, European Molecular Biology Laboratory, Heidelberg, West Germany]. The composition of the protein determined by this method was 49 +/- 2% alpha-helix, 20 +/- 4% beta-sheet, and 31 +/- 3% remainder. This composition changes when the protein is allowed to bind Kemptide , a synthetic peptide substrate, with more than half of the disordered portion of the protein taking the form of beta-sheet. A certain portion of the alpha-helical structure also appears to move into a beta-sheet form. The near-UV CD spectrum of catalytic subunit shows changes in aromatic amino acid dichroism associated with substrate binding. These changes can be ascribed with a fair degree of certainty to alterations in the orientation of a tyrosine residue at the surface of the protein. These findings are discussed in terms of previous work on induced dichroism in this enzyme with regard to control mechanisms operating at the active site.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1357-62
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Near- and far-ultraviolet circular dichroism of the catalytic subunit of adenosine cyclic 5'-monophosphate dependent protein kinase.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't