Linked Life Data

11151010

Source:http://linkedlifedata.com/resource/pubmed/id/11151010

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-1-26
pubmed:abstractText
A novel method is proposed to predict whether two domains connected by a helical link can mutually reorient themselves, as well as where the helix can be distorted to allow the domain-domain movements. The method, based on analysis of the variation of the a.d.p. values along the helix link, is applied to three proteins--calmodulin, lysozyme, and hemagglutinin--for which both the domain-domain flexibility and the helix fragment responsible for it are well documented. The helix regions that are variously distorted to permit domain-domain reorientation are well predicted. The method is also applied to colicin Ia and shows that an inter-domain rearrangement can take place as previously postulated. The prediction of the helix breaking point should prove useful in interpreting structural data and in defining the domain borders automatically for proteins built by domains connected by helical links.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0887-3585
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
390-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Detection of breaking points in helices linking separate domains.
pubmed:affiliation
Department of General Chemistry, University of Pavia, Pavia, Italy. carugo@icgeb.trieste.it
pubmed:publicationType
Journal Article, Comparative Study