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© Research
Publication : Journal of the American Chemical Society

The mechanism of denaturation and the unfolded state of the α-helical membrane-associated protein Mistic

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of the American Chemical Society - 04 Dec 2013

Jacso T, Bardiaux B, Broecker J, Fiedler S, Baerwinkel T, Mainz A, Fink U, Vargas C, Oschkinat H, Keller S, Reif B

Link to Pubmed [PMID] – 24261476

J. Am. Chem. Soc. 2013 Dec;135(50):18884-91

In vitro protein-folding studies using chemical denaturants such as urea are indispensible in elucidating the forces and mechanisms determining the stability, structure, and dynamics of water-soluble proteins. By contrast, α-helical membrane-associated proteins largely evade such approaches because they are resilient to extensive unfolding. We have used optical and NMR spectroscopy to provide an atomistic-level dissection of the effects of urea on the structure and dynamics of the α-helical membrane-associated protein Mistic as well as its interactions with detergent and solvent molecules. In the presence of the zwitterionic detergent lauryl dimethylamine oxide, increasing concentrations of urea result in a complex sequence of conformational changes that go beyond simple two-state unfolding. Exploiting this finding, we report the first high-resolution structural models of the urea denaturation process of an α-helical membrane-associated protein and its completely unfolded state, which contains almost no regular secondary structure but nevertheless retains a topology close to that of the folded state.

http://www.ncbi.nlm.nih.gov/pubmed/24261476