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.
Publication types
- Research Support, N.I.H., Intramural
- Research Support, Non-U.S. Gov't
MeSH terms
- Bacterial Proteins / chemistry*
- Bacterial Proteins / genetics
- Bacterial Proteins / metabolism
- Binding Sites
- Cold Temperature
- Cytotoxins / chemistry*
- Cytotoxins / genetics
- Cytotoxins / metabolism
- DNA, Bacterial / chemistry*
- DNA, Bacterial / genetics
- DNA, Bacterial / metabolism
- Enterococcus faecalis / genetics
- Enterococcus faecalis / metabolism*
- Escherichia coli / genetics
- Models, Molecular
- Molecular Conformation
- Nuclear Magnetic Resonance, Biomolecular
- Promoter Regions, Genetic
- Protein Binding
- Protein Denaturation
- Protein Folding
- Protein Multimerization
- Protein Unfolding
- Recombinant Proteins / chemistry
- Recombinant Proteins / genetics
- Recombinant Proteins / metabolism
Substances
- Bacterial Proteins
- Cytotoxins
- DNA, Bacterial
- Recombinant Proteins
Associated data
- PDB/2LY
- PDB/2LYJ
- PDB/2LYK
- PDB/2LYL
- PDB/2LYP
- PDB/2LYQ
- PDB/2LYS