Linked Life Data

1505002

Source:http://linkedlifedata.com/resource/pubmed/id/1505002

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6-7
pubmed:dateCreated
1992-9-23
pubmed:abstractText
The linker regions of the central helices of calmodulin and of troponin C are observed to be alpha-helices in crystal and in solution. However, these linkers are predicted to be non-helical by standard algorithms. Further, there is strong evidence that when calmodulin interacts with some of its targets this linker helix bends. The linker appears to be delicately balanced between helical and non-helical conformations. A review of this subject suggests that one can anticipate more unpredicted conformations for the central helices of the score of other proteins that have four EF-hand domains.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0143-4160
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
363-76
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
The linker of calmodulin--to helix or not to helix.
pubmed:affiliation
Department of Biology, University of Virginia, Charlottesville.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Review