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

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

J. Am. Chem. Soc. 135, 18884-18891 (2013)
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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, a-helical membrane-associated proteins largely evade such approaches because they are resilient to extensive unfolding We have used of the alpha-helical membrane-associated protein Mistic as well as dissection of the effects of urea on the structure and dynamics optical and NMR spectroscopy to provide an atomistic-level 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 alpha-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.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Triple-resonance Experiments; Secondary Structure; Transmembrane Helices; Circular-dichroism; Hydrogen-bonds; Urea; Nmr; Stability; Expression; Spectroscopy
ISSN (print) / ISBN 0002-7863
e-ISSN 1520-5126
Quellenangaben Volume: 135, Issue: 50, Pages: 18884-18891 Article Number: , Supplement: ,
Publisher American Chemical Society (ACS)
Reviewing status Peer reviewed