Ontology highlight
ABSTRACT:
SUBMITTER: Jaremko M
PROVIDER: S-EPMC5521822 | biostudies-literature | 2013 Apr
REPOSITORIES: biostudies-literature
Jaremko Mariusz M Jaremko Łukasz Ł Kim Hai-Young HY Cho Min-Kyu MK Schwieters Charles D CD Giller Karin K Becker Stefan S Zweckstetter Markus M
Nature chemical biology 20130210 4
Protein folding and unfolding are crucial for a range of biological phenomena and human diseases. Defining the structural properties of the involved transient species is therefore of prime interest. Using a combination of cold denaturation with NMR spectroscopy, we reveal detailed insight into the unfolding of the homodimeric repressor protein CylR2. Seven three-dimensional structures of CylR2 at temperatures from 25 °C to -16 °C reveal a progressive dissociation of the dimeric protein into a na ...[more]