Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1991-11-13
|
| pubmed:abstractText |
The interaction which stabilizes the intermediate state of the protein folding and/or unfolding is important for understanding the structure formation mechanism of proteins. The partitioning of a hydrophobic fluorescence probe, pyrene, into the core of a 'molten globule' structure of bovine carbonic anhydrase B was measured, revealing a partition coefficient of about 10(4). The result leads to the conclusion that the compact structure of the molten-globule state is formed by the hydrophobic interaction, as detergent micelles are formed by the same interaction.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0301-4622
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
40
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
217-22
|
| pubmed:dateRevised |
2003-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:1912287-Animals,
pubmed-meshheading:1912287-Carbonic Anhydrases,
pubmed-meshheading:1912287-Cattle,
pubmed-meshheading:1912287-Circular Dichroism,
pubmed-meshheading:1912287-Fluorescent Dyes,
pubmed-meshheading:1912287-Protein Conformation,
pubmed-meshheading:1912287-Pyrenes,
pubmed-meshheading:1912287-Spectrometry, Fluorescence
|
| pubmed:year |
1991
|
| pubmed:articleTitle |
Hydrophobic core of molten-globule state of bovine carbonic anhydrase B.
|
| pubmed:affiliation |
Tokyo University of Agriculture and Technology, Faculty of Technology, Japan.
|
| pubmed:publicationType |
Journal Article
|