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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1998-7-10
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pubmed:abstractText |
Protein sequence comparison has become a major tool for biologists. Various methods have been designed in order to reveal even remote homologies among proteins. Sequence analyses are powerful, but the lower the identity score, the more skill and time are required to perform them accurately. While necessary to confirm the sequence comparison through the potential of mean force, sequence alignment and molecular modelling are still tedious and time-consuming tasks.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
1367-4803
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
206-11
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9545453-Algorithms,
pubmed-meshheading:9545453-Amino Acid Sequence,
pubmed-meshheading:9545453-Computational Biology,
pubmed-meshheading:9545453-Models, Molecular,
pubmed-meshheading:9545453-Molecular Sequence Data,
pubmed-meshheading:9545453-Protein Conformation,
pubmed-meshheading:9545453-Proteins,
pubmed-meshheading:9545453-Sequence Alignment,
pubmed-meshheading:9545453-Sequence Homology, Amino Acid,
pubmed-meshheading:9545453-Software
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pubmed:year |
1998
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pubmed:articleTitle |
Incremental threading optimization (TITO) to help alignment and modelling of remote homologues.
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pubmed:affiliation |
Systèmes Moléculaires et Biologie Structurale, Laboratoire de Minéralogie-Cristallographie, Universités Paris, Cedex, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|