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Cooperativity of a protein folding reaction probed at multiple chain positions by real-time 2D NMR spectroscopy.

Title data

Steegborn, Clemens ; Schneider-Hassloff, Henriette ; Zeeb, Markus ; Balbach, Jochen:
Cooperativity of a protein folding reaction probed at multiple chain positions by real-time 2D NMR spectroscopy.
In: Biochemistry. Vol. 39 (11 July 2000) Issue 27 . - pp. 7910-7919.
ISSN 0006-2960
DOI: https://doi.org/10.1021/bi000270u

Abstract in another language

The refolding reaction of S54G/P55N ribonuclease T1 is a two-step process, where fast formation of a partly folded intermediate is followed by the slow reaction to the native state, limited by a trans --> cis isomerization of Pro39. The hydrodynamic radius of this kinetic folding intermediate was determined by real-time diffusion NMR spectroscopy. Its folding to the native state was monitored by a series of 128 very fast 2D (15)N-HMQC spectra, to observe the kinetics of 66 individual backbone amide probes. We find that the intermediate is as compact as the native protein with many native chemical shifts. All 66 analyzed amide probes follow the rate-limiting prolyl isomerization, which indicates that this cooperative refolding reaction is fully synchronized. The stability of the folding intermediate was determined from the protection factors of 45 amide protons derived from a competition between refolding and H/D exchange. The intermediate has already gained 40% of the Gibbs free energy of refolding with many protected amides in not-yet-native regions.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 10891071
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Clemens Steegborn
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 13 Apr 2015 08:03
Last Modified: 13 Apr 2015 08:03
URI: https://eref.uni-bayreuth.de/id/eprint/10096