Literature DB >> 15723639

Millisecond protein folding studied by NMR spectroscopy.

Markus Zeeb1, Jochen Balbach.   

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 microsecond-to-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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Year:  2005        PMID: 15723639     DOI: 10.2174/0929866053005917

Source DB:  PubMed          Journal:  Protein Pept Lett        ISSN: 0929-8665            Impact factor:   1.890


  3 in total

1.  Assignment of paramagnetic (15)N-HSQC spectra by heteronuclear exchange spectroscopy.

Authors:  Michael John; Madeleine J Headlam; Nicholas E Dixon; Gottfried Otting
Journal:  J Biomol NMR       Date:  2006-11-10       Impact factor: 2.835

Review 2.  NMR spectroscopy brings invisible protein states into focus.

Authors:  Andrew J Baldwin; Lewis E Kay
Journal:  Nat Chem Biol       Date:  2009-11       Impact factor: 15.040

3.  Recognition of T-rich single-stranded DNA by the cold shock protein Bs-CspB in solution.

Authors:  Markus Zeeb; Klaas E A Max; Ulrich Weininger; Christian Löw; Heinrich Sticht; Jochen Balbach
Journal:  Nucleic Acids Res       Date:  2006-09-06       Impact factor: 16.971

  3 in total

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