Linked Life Data

9223187

Source:http://linkedlifedata.com/resource/pubmed/id/9223187

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-8-1
pubmed:abstractText
Computational structure prediction of streptavidin-peptide complexes for known recognition sequences and a number of random di-, tri-, and tetrapeptides has been conducted, and mechanisms of peptide recognition with streptavidin have been investigated by a new computational protocol. The structural consensus criterion, which is computed from multiple docking simulations and measures the accessibility of the dominant binding mode, identifies recognition motifs from a set of random peptide sequences, whereas energetic analysis is less discriminatory. The predicted conformations of recognition tripeptide and tetrapeptide sequences are also in structural harmony and composed of peptide fragments that are individually unfrustrated in their bound conformation, resulting in a minimally frustrated energy landscape for recognition peptides.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0887-3585
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
421-33
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Structural consensus in ligand-protein docking identifies recognition peptide motifs that bind streptavidin.
pubmed:affiliation
Agouron Pharmaceuticals, Inc., San Diego, California 92121, USA.
pubmed:publicationType
Journal Article