Linked Life Data

8672716

Source:http://linkedlifedata.com/resource/pubmed/id/8672716

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-8-13
pubmed:abstractText
The regulatory peptides Phk13 (301-327) and a modified form of Phk5 (342-367) from the gamma-subunit of glycogen phosphorylase kinase form binary and ternary complexes with both calmodulin and the related muscle protein troponin C. Neither peptide appears to affect to a major extent a fluorescent probe linked to Cys-27 of wheat germ calmodulin. Phk13, but not Phk5, significantly modifies the properties of a probe joined to Cys-98 of troponin C. A comparison by means of radiationless energy transfer of the average separations of Trp-16 of Phk5 from specific groups in the N- and C-terminal halves of calmodulin and troponin C indicate significant changes upon going from the 1:1 binary complex to the 1:1:1 ternary complex with Phk13. A comparison of the effects of addition of Phk13 to calmodulin, troponin C, and their binary complexes with Phk5 suggests that the conformation of Phk13 is similar in the binary and ternary complexes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0301-4622
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
277-88
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
A comparison of the properties of the binary and ternary complexes formed by calmodulin and troponin C with two regulatory peptides of phosphorylase kinase.
pubmed:affiliation
Department of Chemistry and Biochemistry, University of Maryland, Baltimore 21228, USA.
pubmed:publicationType
Journal Article, Comparative Study