Cold denaturation of a protein dimer monitored at atomic resolution

Mariusz Jaremko, Lukasz 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

25 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)264-270
Number of pages7
JournalNature Chemical Biology
Volume9
Issue number4
DOIs
StatePublished - Apr 1 2013

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

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