Cold denaturation of a protein dimer monitored at atomic resolution

Mariusz Jaremko, Łukasz Jaremko, Hai Young Kim, Min Kyu Cho, Charles D. Schwieters, Karin Giller, Stefan Becker, Markus Zweckstetter*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

31 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)264-270
Number of pages7
JournalNature Chemical Biology
Issue number4
StatePublished - Apr 2013
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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