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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1998-11-6
|
| pubmed:abstractText |
Many small, monomeric proteins fold with simple two-state kinetics and show wide variation in folding rates, from microseconds to seconds. Thus, stable intermediates are not a prerequisite for the fast, efficient folding of proteins and may in fact be kinetic traps and slow the folding process. Using recent studies, can we begin to search for trends which may lead to a better understanding of the protein folding process?
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
1359-0278
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
3
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
R81-91
|
| pubmed:dateRevised |
2005-11-16
|
| pubmed:meshHeading |
pubmed-meshheading:9710577-Dimerization,
pubmed-meshheading:9710577-Kinetics,
pubmed-meshheading:9710577-Models, Molecular,
pubmed-meshheading:9710577-Protein Folding,
pubmed-meshheading:9710577-Protein Structure, Secondary,
pubmed-meshheading:9710577-Proteins,
pubmed-meshheading:9710577-Thermodynamics
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
How do small single-domain proteins fold?
|
| pubmed:affiliation |
Chemical Laboratory, University of Cambridge, UK. sej13@cam.ac.uk
|
| pubmed:publicationType |
Journal Article,
Review
|