Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1989-8-14
pubmed:abstractText
A method of protein structure comparison developed previously is extended to incorporate other aspects of protein structure in addition to the inter-atomic vectors on which it was originally based. Each additional aspect, which induced hydrogen bonding, solvent exposure, torsional angles and sequence, was introduced separately and evaluated for its ability to improve alignment quality. The components were then combined, suitably weighted, to produce a more holistic comparison method. The method was tested on a group of remotely related beta/alpha type proteins that share a common feature in their overall chain fold. The results indicated that while the original inter-atomic vector component was sufficient to give the correct alignment of most pairs of topologically equivalent proteins, the inclusion of hydrogen bonds, torsion angles and a measure of solvent exposure led to improvements in the more difficult comparisons. Consideration of amino acid properties, including hydrophobicity, had no beneficial effect. The failure of the latter component was not unexpected considering the almost total lack of sequence similarity among the proteins considered.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0269-2139
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
505-19
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
A holistic approach to protein structure alignment.
pubmed:affiliation
Laboratory of Mathematical Biology, National Institute for Medical Research, The Ridgeway, London, UK.
pubmed:publicationType
Journal Article, Comparative Study