Millisecond protein folding studied by NMR spectroscopy.
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.
Zeeb
Markus
M
Laboratorium für Biochemie, Universität Bayreuth, D-95440 Bayreuth, Germany.
Balbach
Jochen
J
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D008433:Mathematics; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D020673:Protein Renaturation; D014508:Urea / Q000737:chemistry
D001426:Bacterial Proteins; C077188:cold-shock protein CspB, Bacteria; D014508:Urea