期刊
NATURE CHEMISTRY
卷 11, 期 11, 页码 1058-1066出版社
NATURE RESEARCH
DOI: 10.1038/s41557-019-0329-3
关键词
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资金
- NSF [STC-1231306]
- NIH [GM123159, GM124149]
- David and Lucile Packard Foundation
- UC Office of the President Laboratory Fees Research Program [LFR-17-476732]
- Intramural Research Program of the National Institute of Diabetes and Digestive and Kidney Diseases
- Ruth L. Kirschstein National Research Service Award [F32 HL129989]
- US Department of Energy, Basic Energy Sciences, Office of Science [DE-AC02-06CH11357]
- NIH National Institute of General Medical Sciences [R24GM111072]
- NIH/NIDDK
Correlated motions of proteins are critical to function, but these features are difficult to resolve using traditional structure determination techniques. Time-resolved X-ray methods hold promise for addressing this challenge, but have relied on the exploitation of exotic protein photoactivity, and are therefore not generalizable. Temperature jumps, through thermal excitation of the solvent, have been utilized to study protein dynamics using spectroscopic techniques, but their implementation in X-ray scattering experiments has been limited. Here, we perform temperature-jump small- and wide-angle X-ray scattering measurements on a dynamic enzyme, cyclophilin A, demonstrating that these experiments are able to capture functional intramolecular protein dynamics on the microsecond timescale. We show that cyclophilin A displays rich dynamics following a temperature jump, and use the resulting time-resolved signal to assess the kinetics of conformational changes. Two relaxation processes are resolved: a fast process is related to surface loop motions, and a slower process is related to motions in the core of the protein that are critical for catalytic turnover.
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