Wenk, Martina and Jaenicke, Rainer and Mayr, Eva-Maria (1998) Kinetic stabilisation of a modular protein by domain interactions. FEBS LETTERS, 438 (1-2). pp. 127-130. ISSN 0014-5793,
Full text not available from this repository. (Request a copy)Abstract
Protein S, a two-domain spore coat protein from Myxococcus xanthus, is structurally related to eye-lens beta gamma-crystallins. No natural monomeric one-domain member of this protein superfamily is known. To determine the stability of the single domains and to explain the ubiquitous domain duplication, the isolated domains of protein S were constructed. The N-domain is thermodynamically more stable than the C-domain, In intact protein S, domain interactions lead to an apparent decrease in stability of the N-terminal domain, whereas the C-terminal domain is stabilised, In contrast, unfolding kinetics of both domains are decreased 100-fold due to interactions in the complete molecule. (C) 1998 Federation of European Biochemical Societies.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | BETA-GAMMA-CRYSTALLINS; SPORE COAT PROTEIN; EYE LENS; RNA-POLYMERASE; B-CRYSTALLIN; CLONED GENES; EXPRESSION; EVOLUTION; beta gamma-crystallin; domain folding; differential scanning calorimetry; kinetic stabilization; two-domain protein; domain interaction |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 18 Apr 2023 10:29 |
| Last Modified: | 18 Apr 2023 10:29 |
| URI: | https://pred.uni-regensburg.de/id/eprint/49410 |
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