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Microsecond folding of the cold shock protein measured by a pressure-jump technique

Title data

Jacob, Maik H. ; Holtermann, Georg ; Perl, Dieter ; Reinstein, Jochen ; Schindler, Thomas ; Geeves, Michael A. ; Schmid, Franz X.:
Microsecond folding of the cold shock protein measured by a pressure-jump technique.
In: Biochemistry. Vol. 38 (1999) Issue 10 . - pp. 2882-2891.
ISSN 1520-4995
DOI: https://doi.org/10.1021/bi982487i

Abstract in another language

A pressure-jump apparatus was employed in investigating the kinetics of protein unfolding and refolding. In the reaction cell, the pressure can be increased or decreased by 100-160 bar within 50-100 microseconds and then held constant. Thus, unfolding and refolding reactions in the time range from 70 microseconds to 70 s can be followed with this technique. Measurements are possible in the transition regions of thermally or denaturant-induced folding in a wide range of temperatures and solvent conditions. We used this pressure-jump method to determine the temperature dependence of the rate constants of unfolding and refolding of the cold shock protein of Bacillus subtilis and of three variants thereof with Phe --> Ala substitutions in the central beta-sheet region. For all variants, the change in heat capacity occurred in refolding between the unfolded and activated states, suggesting that the overall native-like character of the activated state of folding was not changed by the deletion of individual Phe side chains. The Phe27Ala mutation affected the rate of unfolding only; the Phe15Ala and Phe17Ala mutations changed the kinetics of both unfolding and refolding. Although the activated state of folding of the cold shock protein is overall native-like, individual side chains are still in a non-native environment.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 10074340
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Professor Biochemistry - Univ.-Prof. Dr. Franz Xaver Schmid
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 > Professorship Biochemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 27 May 2015 06:51
Last Modified: 20 Apr 2022 11:51
URI: https://eref.uni-bayreuth.de/id/eprint/14332