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2007 | 54 | 4 | 769-775
Article title

15N magnetic relaxation study of backbone dynamics of the ribosome-associated cold shock response protein Yfia of Escherichia coli

Content
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EN
Abstracts
EN
In the solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli in the free state two structural segments can be distinguished: a well structured, rigid N-terminal part displaying a βαβββα topology and a flexible C-terminal tail comprising last 20 amino-acid residues. The backbone dynamics of Yfia protein was studied by 15N nuclear magnetic relaxation at three magnetic fields and analyzed using model-free approach. The overall diffusional tumbling of the N-terminal part is strongly anisotropic with a number of short stretches showing increased mobility either on a subnanosecond time scale, or a micro- to millisecond time scale, or both. In contrast, the unstructured polypeptide chain of the C-terminal part, which cannot be regarded as a rigid structure, shows the predominance of fast local motions over slower ones, both becoming faster closer to the C-terminus.
Publisher

Year
Volume
54
Issue
4
Pages
769-775
Physical description
Dates
published
2007
received
2007-07-25
revised
2007-10-02
accepted
2007-10-26
(unknown)
2007-10-31
Contributors
author
  • Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warszawa, Poland
author
  • Department of Structural and Medicinal Biochemistry, Centre of Medical Biotechnology, University of Duisburg-Essen, Essen, German
  • Department of Structural and Medicinal Biochemistry, Centre of Medical Biotechnology, University of Duisburg-Essen, Essen, German
  • Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warszawa, Poland
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv54p769kz
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