@article{3e0d57e33cac45288e1ff1efdaf22737,
title = "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.",
author = "Mariusz Jaremko and {\L}ukasz Jaremko and Kim, {Hai Young} and Cho, {Min Kyu} and Schwieters, {Charles D.} and Karin Giller and Stefan Becker and Markus Zweckstetter",
note = "Funding Information: We thank N. Rezaei-Ghaleh for useful discussions. This work was supported by the START and Ventures Programmes of Foundation for Polish Science (Fundacja na rzecz Nauki Polskiej; http://www.fnp.org.pl/) operated within the Innovative Economy Operational Programme (IE OP) 2007-2013 within European Regional Development Fund (L.J. and M.J.), the Iuventus Plus project no. IP2011 019471 from Polish Ministry of Sciences and Higher Education (M.J.) and the Cluster of Excellence and Deutsche Forschungsgemeinschaft Research Center “Nanoscale Microscopy and Molecular Physiology of the Brain” (to M.Z.). C.D.S. was supported by the Intramural Research Program of the Center for Information Technology at the US National Institutes of Health.",
year = "2013",
month = apr,
doi = "10.1038/nchembio.1181",
language = "English (US)",
volume = "9",
pages = "264--270",
journal = "Nature Chemical Biology",
issn = "1552-4450",
publisher = "Nature Research",
number = "4",
}
