| pubmed-article:10998051 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10998051 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
| pubmed-article:10998051 | lifeskim:mentions | umls-concept:C0023317 | lld:lifeskim |
| pubmed-article:10998051 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:10998051 | lifeskim:mentions | umls-concept:C1705241 | lld:lifeskim |
| pubmed-article:10998051 | lifeskim:mentions | umls-concept:C1705242 | lld:lifeskim |
| pubmed-article:10998051 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:10998051 | pubmed:dateCreated | 2000-11-13 | lld:pubmed |
| pubmed-article:10998051 | pubmed:abstractText | Lens alphaA- and alphaB-crystallin have been reported to act differently in their protection against nonthermal destabilization of proteins. The nature of this difference, however, is not completely understood. Therefore we used a combination of thermally and solvent-induced structural changes to investigate the difference in the secondary, tertiary and quaternary structures of alphaA- and alphaB-crystallin. We demonstrate the relationship between the changes in the tertiary and quaternary structures for both polypeptides. Far-ultraviolet circular dichroism revealed that the secondary structure of alphaB-crystallin is more stable than that of alphaA-crystallin, and the temperature-induced secondary structure changes of both polypeptides are partially reversible. Tryptophan fluorescence revealed two distinct transitions for both alphaA- and alphaB-crystallin. Compared to alphaB-crystallin, both transitions of alphaA-crystallin occurred at higher temperature. The changes in the hydrophobicity are accompanied by changes in the quaternary structure and are biphasic, as shown by bis-1-anilino-8-naphthalenesulfonate fluorescence and sedimentation velocity. These phenomena explain the difference in the chaperone capacity of alphaA- and alphaB-crystallin carried out at different temperatures. The quaternary structure of alpha-crystallin is more stable than that of alphaA- and alphaB-crystallin. The latter has a strong tendency to dissociate under thermal or solvent destabilization. This phenomenon is related to the difference in subunit organization of alphaA- and alphaB-crystallin where both hydrophobic and ionic interactions are involved. We find that an important subunit rearrangement of alphaA-crystallin takes place once the molecule is destabilized. This subunit rearrangement is a requisite phenomenon for maintaining alpha-crystallin in its globular form and as a stable complex. On the base of our results, we suggest a four-state model describing the folding and dissociation of alphaA- and alphaB-crystallin better than a three-state model [Sun et al. (1999) J. Biol. Chem. 274, 34067-34071]. | lld:pubmed |
| pubmed-article:10998051 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10998051 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10998051 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10998051 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10998051 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10998051 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10998051 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10998051 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10998051 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:10998051 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:10998051 | pubmed:author | pubmed-author:ClauwaertJJ | lld:pubmed |
| pubmed-article:10998051 | pubmed:author | pubmed-author:AertsTT | lld:pubmed |
| pubmed-article:10998051 | pubmed:author | pubmed-author:BackmannJJ | lld:pubmed |
| pubmed-article:10998051 | pubmed:author | pubmed-author:VanhoudtJJ | lld:pubmed |
| pubmed-article:10998051 | pubmed:author | pubmed-author:AbgarSS | lld:pubmed |
| pubmed-article:10998051 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10998051 | pubmed:volume | 267 | lld:pubmed |
| pubmed-article:10998051 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10998051 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10998051 | pubmed:pagination | 5916-25 | lld:pubmed |
| pubmed-article:10998051 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:10998051 | pubmed:meshHeading | pubmed-meshheading:10998051... | lld:pubmed |
| pubmed-article:10998051 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10998051 | pubmed:articleTitle | The structural differences between bovine lens alphaA- and alphaB-crystallin. | lld:pubmed |
| pubmed-article:10998051 | pubmed:affiliation | Biophysics Research Group, Department of Biochemistry, University of Antwerp, Belgium. | lld:pubmed |
| pubmed-article:10998051 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10998051 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:10998051 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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