SIEBENDRITT, R and SHARMA, AK and RUDOLPH, R and JAENICKE, R (1991) ANALYSIS OF PROTEIN FOLDING BY FAST PROTEIN LIQUID-CHROMATOGRAPHY - MODULAR DOMAIN FOLDING OF GAMMA-II-CRYSTALLIN FROM CALF EYE-LENS. BIOLOGICAL CHEMISTRY HOPPE-SEYLER, 372 (1). pp. 23-26. ISSN 0177-3593,
Full text not available from this repository.Abstract
Fast protein liquid chromatography was effectively applied to analyse the folding mechanism of gamma-II-crystallin from calf eye-lens. The protein undergoes a bimodal folding/unfolding transition, according to a three-state model: N half-arrow-right-over-half-arrow-left I half-arrow-right-over-half-arrow-left D where N, I, and D stand for the native, intermediate and denatured states (R. Rudolp, R. Siebendritt, G. NeBlauer, A.K. Sharma & R. Jaenicke (1990) Proc. Natl. Acad. Sci. USA 87, 4625-4629). Using Superose 12 HR 10/30, the intermediate with the N-terminal domain intact, and the C-terminal domain unfolded, could be separated from the native protein. The N --> I transition is sufficiently slow to allow kinetic measurements, following the variation of the respective peak-heights during denaturation/renaturation. The corresponding relaxation times are in agreement with kinetic data based on the change in fluorescence emission accompanying the N half-arrow-right-over-half-arrow-left I transition.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ; CRYSTALLIN; DOMAIN PROTEIN; EYE-LENS; FOLDING; FPLC |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:46 |
| URI: | https://pred.uni-regensburg.de/id/eprint/55117 |
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