期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 59, 期 27, 页码 11108-11114出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202003527
关键词
conformational entropy; membrane proteins; NMR spectroscopy; protein folding; side-chain dynamics
资金
- G. Harold and Leila Y. Mathers Foundation
- National Science Foundation [ACI-1548562]
- DOE Office of Science [DE-SC0012704]
- National Institute of Health, National Institute of General Medical Sciences (NIGMS) through a Biomedical Technology Research Resource P41 grant [P41GM111244]
- DOE Office of Biological and Environmental Research [KP1605010]
- NIH [T32 GM008275, T32 GM008403]
- [R01 GM079440]
The internal motions of integral membrane proteins have largely eluded comprehensive experimental characterization. Here the fast side-chain dynamics of the alpha-helical sensory rhodopsin II and the beta-barrel outer membrane protein W have been investigated in lipid bilayers and detergent micelles by solution NMR relaxation techniques. Despite their differing topologies, both proteins have a similar distribution of methyl-bearing side-chain motion that is largely independent of membrane mimetic. The methyl-bearing side chains of both proteins are, on average, more dynamic in the ps-ns timescale than any soluble protein characterized to date. Accordingly, both proteins retain an extraordinary residual conformational entropy in the folded state, which provides a counterbalance to the absence of the hydrophobic effect. Furthermore, the high conformational entropy could greatly influence the thermodynamics underlying membrane-protein functions, including ligand binding, allostery, and signaling.
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