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

• Authors: Igor Zhukov , Peter Bayer , Beate Schölermann , Andrzej Ejchart
• Languages of publication: 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.

Keywords

EN

anisotropic overall molecular diffusion; model-free approach; 15N NMR spectroscopy; stress adaptation; disordered polypetide chain motion; protein Y

• Journal: Acta Biochimica Polonica
• Year: 2007
• Volume: 54
• Issue: 4
• Pages: 769-775

Dates

published

2007

received

2007-07-25

revised

2007-10-02

accepted

2007-10-26

(unknown)

2007-10-31

Contributors

author

Igor Zhukov

• Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warszawa, Poland

author

Peter Bayer

• Department of Structural and Medicinal Biochemistry, Centre of Medical Biotechnology, University of Duisburg-Essen, Essen, German

author

Beate Schölermann

• Department of Structural and Medicinal Biochemistry, Centre of Medical Biotechnology, University of Duisburg-Essen, Essen, German

author

Andrzej Ejchart

• Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warszawa, Poland

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