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Water contributes actively to the rapid crossing of a protein unfolding barrier

Title data

Jacob, Maik H. ; Saudan, Christophe ; Holtermann, Georg ; Martin, Andreas ; Perl, Dieter ; Merbach, André E. ; Schmid, Franz X.:
Water contributes actively to the rapid crossing of a protein unfolding barrier.
In: Journal of Molecular Biology. Vol. 318 (3 May 2002) Issue 3 . - pp. 837-845.
ISSN 0022-2836
DOI: https://doi.org/10.1016/S0022-2836(02)00165-1

Official URL: Volltext

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Abstract in another language

The cold-shock protein CspB folds rapidly in a N <= => U two-state reaction via a transition state that is about 90% native in its interactions with denaturants and water. This suggested that the energy barrier to unfolding is overcome by processes occurring in the protein itself, rather than in the solvent. Nevertheless, CspB unfolding depends on the solvent viscosity. We determined the activation volumes of unfolding and refolding by pressure-jump and high-pressure stopped-flow techniques in the presence of various denaturants. The results obtained by these methods agree well. The activation volume of unfolding is positive (Delta V(++)(NU)=16(+/-4) ml/mol) and virtually independent of the nature and the concentration of the denaturant. We suggest that in the transition state the protein is expanded and water molecules start to invade the hydrophobic core. They have, however, not yet established favorable interactions to compensate for the loss of intra-protein interactions. The activation volume of refolding is positive as well (Delta V(++)(NU)=53(+/-6) ml/mol) and, above 3 M urea, independent of the concentration of the denaturant. At low concentrations of urea or guanidinium thiocyanate, Delta V(++)(UN) decreases significantly, suggesting that compact unfolded forms become populated under these conditions.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 12054827
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: 28 Apr 2015 09:28
Last Modified: 11 Feb 2016 16:02
URI: https://eref.uni-bayreuth.de/id/eprint/10842