Structural highlights
Function
Q8VL32_ENTFL
Publication Abstract from PubMed
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 degrees C to -16 degrees 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.
Cold denaturation of a protein dimer monitored at atomic resolution.,Jaremko M, Jaremko L, Kim HY, Cho MK, Schwieters CD, Giller K, Becker S, Zweckstetter M Nat Chem Biol. 2013 Feb 10. doi: 10.1038/nchembio.1181. PMID:23396077[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jaremko M, Jaremko L, Kim HY, Cho MK, Schwieters CD, Giller K, Becker S, Zweckstetter M. Cold denaturation of a protein dimer monitored at atomic resolution. Nat Chem Biol. 2013 Feb 10. doi: 10.1038/nchembio.1181. PMID:23396077 doi:http://dx.doi.org/10.1038/nchembio.1181
