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Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
|
pubmed:dateCreated |
1996-10-18
|
pubmed:abstractText |
Structural and mechanistic information, sequence comparisons, and site-directed mutagenesis data continue to provide a basis for the rational design of new protein functions and the alteration of existing functions. Random mutagenesis and 'directed evolution' approaches, however, are making significant headway in solving protein engineering problems, proving highly practical for tuning properties such as enzyme substrate specificity.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0959-440X
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
6
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
513-8
|
pubmed:dateRevised |
2005-11-16
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pubmed:meshHeading |
pubmed-meshheading:8794158-Binding Sites,
pubmed-meshheading:8794158-Directed Molecular Evolution,
pubmed-meshheading:8794158-Green Fluorescent Proteins,
pubmed-meshheading:8794158-Luminescent Proteins,
pubmed-meshheading:8794158-Protein Engineering,
pubmed-meshheading:8794158-Proteins,
pubmed-meshheading:8794158-Structure-Activity Relationship,
pubmed-meshheading:8794158-Substrate Specificity
|
pubmed:year |
1996
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pubmed:articleTitle |
Engineering new functions and altering existing functions.
|
pubmed:affiliation |
Division of Chemistry and Chemical Engineering, 210-41, California Institute of Technology, Pasadena, CA 91125, USA.
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pubmed:publicationType |
Journal Article,
Review
|