Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
8
|
| pubmed:dateCreated |
1998-8-31
|
| pubmed:abstractText |
Protein engineering studies show that conformations in the folding transition state ensemble can be structurally polarized. In two SH3 beta-sheet domains, the formation of hydrophobic contacts goes hand in hand with the formation of the solvated distal loop beta-turn, while large parts of the molecule remain unstructured in the ensemble.
|
| pubmed:commentsCorrections | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
1072-8368
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
5
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
662-5
|
| pubmed:dateRevised |
2001-11-26
|
| pubmed:meshHeading | |
| pubmed:year |
1998
|
| pubmed:articleTitle |
Satisfying turns in folding transitions.
|
| pubmed:publicationType |
Comment,
News
|