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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1997-7-14
|
| pubmed:abstractText |
gammaB-crystallin from vertebrate eye lens is an all beta-sheet two-domain protein with a high degree of intrachain symmetry. Its N and C-terminal domains show high levels of sequence similarity and structural identity. In natural gammaB-crystallin, the domains fold independently. The recombinantly expressed isolated domains are stable monomeric proteins, which do not associate spontaneously to form a gammaB-like dimer. In contrast to their identical folding topology, the two domains obviously follow different folding mechanisms. While the two-state model is valid for the C-terminal domain, the folding behaviour of the N-terminal domain is more complex. The stability of the C-terminal domain is strongly dependent on pH. At pH 2, the C-terminal domain in its isolated form is significantly less stable than within the gammaB-molecule. In contrast, the isolated N-terminal domain does not differ in its stability from the N-terminal domain in wild-type gammaB-crystallin. The strongly decreased stability of the C-terminal domain at acid pH allowed a dissection of the intrinsic stabilities of the domains and their interactions in gammaB-crystallin. At pH 2, domain interactions contribute -16 kJ/mol to the overall stability of gammaB-crystallin.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Crystallins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanidine,
http://linkedlifedata.com/resource/pubmed/chemical/Guanidines,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Urea
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0022-2836
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
6
|
| pubmed:volume |
269
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
260-9
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9191069-Amino Acid Sequence,
pubmed-meshheading:9191069-Circular Dichroism,
pubmed-meshheading:9191069-Crystallins,
pubmed-meshheading:9191069-Dimerization,
pubmed-meshheading:9191069-Guanidine,
pubmed-meshheading:9191069-Guanidines,
pubmed-meshheading:9191069-Models, Molecular,
pubmed-meshheading:9191069-Molecular Sequence Data,
pubmed-meshheading:9191069-Peptide Fragments,
pubmed-meshheading:9191069-Protein Denaturation,
pubmed-meshheading:9191069-Protein Folding,
pubmed-meshheading:9191069-Protein Structure, Secondary,
pubmed-meshheading:9191069-Protein Structure, Tertiary,
pubmed-meshheading:9191069-Recombinant Proteins,
pubmed-meshheading:9191069-Sequence Homology, Amino Acid,
pubmed-meshheading:9191069-Spectrometry, Fluorescence,
pubmed-meshheading:9191069-Spectrophotometry, Ultraviolet,
pubmed-meshheading:9191069-Urea
|
| pubmed:year |
1997
|
| pubmed:articleTitle |
The domains in gammaB-crystallin: identical fold-different stabilities.
|
| pubmed:affiliation |
Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Germany.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|