Linked Life Data

10388841

Source:http://linkedlifedata.com/resource/pubmed/id/10388841

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1999-8-24
pubmed:abstractText
Backbone mimicry by the formation of closed-loop C7, C10 and C13 (mimics of gamma-, beta- and alpha-turns) conformations through side chain-main chain hydrogen bonds by polar groups is a frequent observation in protein structures. A data set of 250 non-homologous and high-resolution protein crystal structures was used to analyze these conformations for their characteristic features. Seven out of the nine polar residues (Ser, Thr, Asn, Asp, Gln, Glu and His) have hydrogen bonding groups in their side chains which can participate in such mimicry and as many as 15% of all these polar residues engage in such conformations. The distributions of dihedral angles of these mimics indicate that only certain combinations of the dihedral angles involved aid the formation of these mimics. The observed examples were categorized into various classes based on these combinations, resulting in well defined motifs. Asn and Asp residues show a very high capability to perform such backbone secondary structural mimicry. The most highly mimicked backbone structure is of the C10 conformation by the Asx residues. The mimics formed by His, Ser, Thr and Glx residues are also discussed. The role of such conformations in initiating the formation of regular secondary structures during the course of protein folding seems significant.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0269-2139
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
447-55
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Secondary structures without backbone: an analysis of backbone mimicry by polar side chains in protein structures.
pubmed:affiliation
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
pubmed:publicationType
Journal Article