rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1997-2-27
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pubmed:databankReference |
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pubmed:abstractText |
The study of DNA polymerases in the Pol l family is central to the understanding of DNA replication and repair. DNA polymerases are used in many molecular biology techniques, including PCR, which require a thermostable polymerase. In order to learn about Pol I function and the basis of thermostability, we undertook structural studies of a new thermostable DNA polymerase.
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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 |
|
pubmed:status |
MEDLINE
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pubmed:month |
Jan
|
pubmed:issn |
0969-2126
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
15
|
pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
95-108
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9016716-Amino Acid Sequence,
pubmed-meshheading:9016716-Binding Sites,
pubmed-meshheading:9016716-Cloning, Molecular,
pubmed-meshheading:9016716-Conserved Sequence,
pubmed-meshheading:9016716-Crystallography, X-Ray,
pubmed-meshheading:9016716-DNA Polymerase I,
pubmed-meshheading:9016716-Enzyme Stability,
pubmed-meshheading:9016716-Exonucleases,
pubmed-meshheading:9016716-Geobacillus stearothermophilus,
pubmed-meshheading:9016716-Hydrogen Bonding,
pubmed-meshheading:9016716-Kinetics,
pubmed-meshheading:9016716-Models, Molecular,
pubmed-meshheading:9016716-Molecular Sequence Data,
pubmed-meshheading:9016716-Protein Binding,
pubmed-meshheading:9016716-Protein Structure, Secondary,
pubmed-meshheading:9016716-Protein Structure, Tertiary,
pubmed-meshheading:9016716-Recombinant Proteins,
pubmed-meshheading:9016716-Sequence Homology, Amino Acid,
pubmed-meshheading:9016716-Software
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pubmed:year |
1997
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pubmed:articleTitle |
Crystal structure of a thermostable Bacillus DNA polymerase I large fragment at 2.1 A resolution.
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pubmed:affiliation |
Department of Biochemistry, Duke University Medical Centre, Durham, NC 27710, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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