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Open Access Green as soon as Postprint is submitted to ZB.
The mechanism of denaturation and the unfolded state of the α-helical membrane-associated protein Mistic.
J. Am. Chem. Soc. 135, 18884-18891 (2013)
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
Publisher
American Chemical Society (ACS)
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)