Abstract
Proteins are involved in virtually every biological process and in order to function, it is necessary for these polypeptide chains to fold into the unique, native conformation. This folding process can take place rapidly. NMR line shape analyses and transverse relaxation measurements allow protein folding studies on a microsecondto- millisecond time scale. Together with an overview of current achievements within this field, we present millisecond protein folding studies by NMR of the cold shock protein CspB from Bacillus subtilis.
Keywords: millisecond protein folding, nmr line shape analysis, r2 relaxation, r2 relaxation dispersion, cold shock protein, cspb
Protein & Peptide Letters
Title: Millisecond Protein Folding Studied by NMR Spectroscopy
Volume: 12 Issue: 2
Author(s): Markus Zeeb and Jochen Balbach
Affiliation:
Keywords: millisecond protein folding, nmr line shape analysis, r2 relaxation, r2 relaxation dispersion, cold shock protein, cspb
Abstract: Proteins are involved in virtually every biological process and in order to function, it is necessary for these polypeptide chains to fold into the unique, native conformation. This folding process can take place rapidly. NMR line shape analyses and transverse relaxation measurements allow protein folding studies on a microsecondto- millisecond time scale. Together with an overview of current achievements within this field, we present millisecond protein folding studies by NMR of the cold shock protein CspB from Bacillus subtilis.
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Cite this article as:
Zeeb Markus and Balbach Jochen, Millisecond Protein Folding Studied by NMR Spectroscopy, Protein & Peptide Letters 2005; 12 (2) . https://dx.doi.org/10.2174/0929866053005917
DOI https://dx.doi.org/10.2174/0929866053005917 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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