Unknown

Dataset Information

0

Cold denaturation of a protein dimer monitored at atomic resolution.


ABSTRACT: 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 native-like monomeric intermediate followed by transition into a highly dynamic, partially folded state. The core of the partially folded state seems critical for biological function and misfolding.

SUBMITTER: Jaremko M 

PROVIDER: S-EPMC5521822 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

Cold denaturation of a protein dimer monitored at atomic resolution.

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]

Similar Datasets

| S-EPMC404062 | biostudies-literature
| S-EPMC9202374 | biostudies-literature
| S-EPMC3071246 | biostudies-literature
| S-EPMC9325448 | biostudies-literature
| S-EPMC3562818 | biostudies-literature
| S-EPMC7733841 | biostudies-literature
| S-EPMC5853651 | biostudies-literature
| S-EPMC4987839 | biostudies-literature
| S-EPMC9072581 | biostudies-literature
| S-EPMC3945965 | biostudies-literature