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Extremely rapid protein folding in the absence of intermediates

Title data

Schindler, Thomas ; Herrler, Michael ; Marahiel, Mohamed A. ; Schmid, Franz X.:
Extremely rapid protein folding in the absence of intermediates.
In: Nature Structural & Molecular Biology. Vol. 2 (August 1995) Issue 8 . - pp. 663-673.
ISSN 1545-9985
DOI: https://doi.org/10.1038/nsb0895-663

Abstract in another language

Here we used the cold-shock protein CspB from Bacillus subtilis to study protein folding at an elementary level. The thermodynamic stability of this small five-stranded beta-barrel protein is low, but unfolding and refolding are extremely rapid reactions. In 0.6 M urea the time constant of refolding is about 1.5 ms, and at the transition midpoint (4 M urea) the folded and unfolded forms equilibrate in less than 100 ms. Both the equilibrium unfolding transition and the folding kinetics are perfectly described by a N<-->U two-state model. The validity of this model was confirmed by several kinetic tests. Folding intermediates could neither be detected at equilibrium nor in the folding kinetics. We suggest that the extremely rapid folding of CspB and the absence of folding intermediates are related phenomena.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 7552728
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Professorship 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: 15 May 2015 08:50
Last Modified: 15 May 2015 08:50
URI: https://eref.uni-bayreuth.de/id/eprint/13476