Source:http://linkedlifedata.com/resource/pubmed/id/19347908
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
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pubmed:dateCreated |
2009-4-21
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pubmed:abstractText |
A designer monomeric protein with a beta alpha beta fold--two parallel beta strands connected by an alpha helix (see structure)--was constructed solely from coded amino acids. The high thermal stability of the structure is due to a large extent to tryptophan-tryptophan interactions between the two beta strands.
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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 |
1521-3773
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
48
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3301-3
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pubmed:meshHeading | |
pubmed:year |
2009
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pubmed:articleTitle |
De novo design of a beta alpha beta motif.
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pubmed:affiliation |
College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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