Wieligmann, Karin and Mayr, Eva-Maria and Jaenicke, Rainer (1999) Folding and self-assembly of the domains of beta B2-crystallin from rat eye lens. JOURNAL OF MOLECULAR BIOLOGY, 286 (4). pp. 989-994. ISSN 0022-2836,
Full text not available from this repository. (Request a copy)Abstract
beta B2-Crystallin from vertebrate eye lens forms domain-swapped dimers, with subunits consisting of two all-beta domains connected by an eight-residue extended Linker peptide. Topologically, the two domains show great similarity; however, they differ widely in their stability. As shown by urea-induced equilibrium unfolding experiments, the isolated monomeric C-terminal domain is more stable than complete beta B2. In contrast, the N-terminal domain exhibits marginal stability only in its dimeric state; upon subunit dissociation, at low protein concentration, unfolding takes place. The folding and association of intact beta B2 follows a sequential uni-bimolecular mechanism according to N-2 reversible arrow 2 I reversible arrow 2U, whereas the isolated domains may be quantitatively described by the two-state model (N reversible arrow U). (C) 1999 Academic Press.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | GAMMA-CRYSTALLIN; PROTEINS; RESOLUTION; EXPRESSION; EVOLUTION; STABILITY; association; crystallins; domains; folding; stability |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 15 Nov 2022 07:47 |
| Last Modified: | 15 Nov 2022 07:47 |
| URI: | https://pred.uni-regensburg.de/id/eprint/48441 |
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