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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1998-1-15
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pubmed:abstractText |
Approximately one third of known protein sequences are related to at least one known protein structure. As a result, an order of magnitude more sequences can be modeled by comparative modeling than there are experimentally determined protein structures. A large fraction of these models has an accuracy approaching that of a low resolution X-ray structure or a medium resolution nuclear magnetic resonance structure. The number of applications where homology modeling has been proven useful is growing rapidly.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
|
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1357-4310
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
270-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9415161-Amino Acid Sequence,
pubmed-meshheading:9415161-Animals,
pubmed-meshheading:9415161-Chymases,
pubmed-meshheading:9415161-Computer Simulation,
pubmed-meshheading:9415161-Crystallography, X-Ray,
pubmed-meshheading:9415161-Mice,
pubmed-meshheading:9415161-Models, Molecular,
pubmed-meshheading:9415161-Molecular Sequence Data,
pubmed-meshheading:9415161-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:9415161-Protein Conformation,
pubmed-meshheading:9415161-Proteins,
pubmed-meshheading:9415161-Serine Endopeptidases,
pubmed-meshheading:9415161-Software,
pubmed-meshheading:9415161-Tryptases
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pubmed:year |
1995
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pubmed:articleTitle |
Comparative protein modeling by satisfaction of spatial restraints.
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pubmed:affiliation |
Rockefeller University, New York, NY 10021-6399, USA. sali@rockvax.rockefeller.edu
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pubmed:publicationType |
Journal Article,
Comparative Study,
Review
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