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Georg Krainer Andreas Hartmann Abhinaya Anandamurugan Pablo Gracia Sandro Keller Michael Schlierf 《Journal of molecular biology》2018,430(4):554-564
Proteins fold on timescales from hours to microseconds. In addition to protein size, sequence, and topology, the environment represents an equally important factor in determining folding speed. This is particularly relevant for proteins that require a lipid membrane or a membrane mimic to fold. However, only little is known about how properties of such a hydrophilic/hydrophobic interface modulate the folding landscape of membrane-interacting proteins. Here, we studied the influence of different membrane-mimetic micellar environments on the folding and unfolding kinetics of the helical-bundle protein Mistic. Devising a single-molecule fluorescence spectroscopy approach, we extracted folding and unfolding rates under equilibrium conditions and dissected the contributions from different detergent moieties to the free-energy landscape. While both polar and nonpolar moieties contribute to stability, they exert differential effects on the free-energy barrier: Hydrophobic burial stabilizes the folded state but not the transition state in reference to a purely aqueous environment; by contrast, zwitterionic headgroup moieties stabilize the folded state and, additionally, lower the free-energy barrier to accelerate the folding of Mistic to achieve ultrafast folding times down to 35 μs. 相似文献
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Sara Roose Russell W. Avramenko Stephen M. J. Pollo James D. Wasmuth Shaali Ame Mio Ayana Martha Betson Piet Cools Daniel Dana Ben P. Jones Zeleke Mekonnen Arianna Morosetti Abhinaya Venkatesan Johnny Vlaminck Matthew L. Workentine Bruno Levecke John S. Gilleard Peter Geldhof 《PLoS neglected tropical diseases》2021,15(9)
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