Linked Life Data

16455751

Source:http://linkedlifedata.com/resource/pubmed/id/16455751

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2006-3-20
pubmed:abstractText
The mobility of a residue on the protein surface is closely linked to its function. The identification of extremely rigid or flexible surface residues can therefore contribute information crucial for solving the complex problem of identifying functionally important residues in proteins. Mobility is commonly measured by B-value data from high-resolution three-dimensional X-ray structures. Few methods predict B-values from sequence. Here, we present PROFbval, the first web server to predict normalized B-values from amino acid sequence. The server handles amino acid sequences (or alignments) as input and outputs normalized B-value and two-state (flexible/rigid) predictions. The server also assigns a reliability index for each prediction. For example, PROFbval correctly identifies residues in active sites on the surface of enzymes as particularly rigid. AVAILABILITY: http://www.rostlab.org/services/profbval CONTACT: profbval@rostlab.org SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1367-4803
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
891-3
pubmed:dateRevised
2010-5-10
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
PROFbval: predict flexible and rigid residues in proteins.
pubmed:affiliation
CUBIC, Department of Biochemistry and Molecular Biophysics, Columbia University, 650 West 168th Street BB217, New York, NY 10032, USA. profbval@rostlab.org
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural