Perl, Dieter and Welker, Christine and Schindler, Thomas and Schröder, Katja and Marahiel, Mohamed A. and Jaenicke, Rainer and Schmid, Franz X. (1998) Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. NATURE STRUCTURAL BIOLOGY, 5 (3). pp. 229-235. ISSN 1072-8368
Full text not available from this repository. (Request a copy)Abstract
The cold shock protein CspB from Bacillus subtilis is only marginally stable, but it folds extremely fast in a simple N reversible arrow U two-state reaction. The corresponding cold shock proteins from the thermophile Bacillus caldolyticus and the hyperthermophile Thermotoga maritima show strongly increased conformational stabilities, but unchanged very fast two-state refolding kinetics. The absence of intermediates in the folding of B. subtilis CspB is thus not a corollary of its low stability. Rather, two-state folding and an unusually native-like activated state of folding seem to be inherent properties of these small all-beta proteins. There is no link between stability and folding rate, and numerous sequence positions exist which can be varied to modulate the stability without affecting the rate and mechanism of folding.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | BACILLUS-SUBTILIS; TRANSITION-STATE; CHYMOTRYPSIN INHIBITOR-2; 2-STATE TRANSITION; LYSOZYME; KINETICS; ACID; MECHANISM; REPRESSOR; STABILITY |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 28 Mar 2023 04:25 |
| Last Modified: | 28 Mar 2023 04:25 |
| URI: | https://pred.uni-regensburg.de/id/eprint/50063 |
Actions (login required)
 |
View Item |
