Mayr, EM and Jaenicke, R and Glockshuber, R (1997) The domains in gamma B-crystallin: Identical fold-different stabilities. JOURNAL OF MOLECULAR BIOLOGY, 269 (2). pp. 260-269. ISSN 0022-2836,
Full text not available from this repository.Abstract
gamma B-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 gamma B-crystallin, the domains fold independently. The recombinantly expressed isolated domains are stable monomeric proteins, which do not associate spontaneously to form a gamma B-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 gamma B-molecule. Ln contrast, the isolated N-terminal domain does not differ in its stability from the N-terminal domain in wild-type gamma B-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 gamma B-crystallin. At pH 2, domain interactions contribute -16 kJ/mol to the overall stability of gamma B-crystallin. (C) 1997 Academic Press Limited.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | X-RAY-ANALYSIS; CALF EYE LENS; II-CRYSTALLIN; ESCHERICHIA-COLI; BETA-CRYSTALLIN; PH-DEPENDENCE; PROTEIN; EXPRESSION; EVOLUTION; DENATURATION; crystallins; protein folding; protein stability; domain association; domain interactions |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:31 |
| URI: | https://pred.uni-regensburg.de/id/eprint/50763 |
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