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

Jacob, M., Holtermann, G., Perl, D., Reinstein, J., Schindler, T., Geeves, M. A., et al. (1999). Microsecond folding of the cold shock protein measured by a pressure jump technique. Biochemistry, 38(10), 2882-2891. doi:10.1021/bi982487i.

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Genre: Journal Article
Alternative Title : Microsecond folding of the cold shock protein measured by a pressure jump technique

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Biochem_38_1999_2882.pdf (Any fulltext), 216KB
 
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 Creators:
Jacob, Maik, Author
Holtermann, Georg, Author
Perl, Dieter, Author
Reinstein, Jochen1, Author           
Schindler, Thomas, Author
Geeves, Michael A., Author
Schmid, Franz X., Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: bacillus-subtilis; Mutation; protein; folding; Shock
 Abstract: 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.

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Language(s): eng - English
 Dates: 1998-12-301998-10-191999-02-131999-02-131999-03-09
 Publication Status: Issued
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 665721
DOI: 10.1021/bi982487i
URI: https://www.ncbi.nlm.nih.gov/pubmed/10074340
Other: 6225
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Title: Biochemistry
Source Genre: Journal
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Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 38 (10) Sequence Number: - Start / End Page: 2882 - 2891 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103