Temperature-jump solution X-ray scattering reveals distinct motions in a dynamic enzyme

Thompson, Michael C.; Barad, Benjamin A.; Wolff, Alexander M.; Sun Cho, Hyun; Schotte, Friedrich; Schwarz, Daniel C.; Anfinrud, Philip; Fraser, James S.

doi:10.1038/s41557-019-0329-3

Temperature-jump solution X-ray scattering reveals distinct motions in a dynamic enzyme

Journal Article · Mon Sep 16 00:00:00 EDT 2019 · Nature Chemistry

DOI:https://doi.org/10.1038/s41557-019-0329-3· OSTI ID:1573394

Thompson, Michael C. ^[1]; Barad, Benjamin A. ^[1]; Wolff, Alexander M. ^[1]; Sun Cho, Hyun ^[2]; Schotte, Friedrich ^[2]; ^[1]; Anfinrud, Philip ^[2]; ^[1]

Univ. of California, San Francisco, CA (United States)
National Inst. of Health (NIH), Bethesda, MD (United States). National Inst. of Diabetes and Digestive and Kidney Diseases, Lab. of Chemical Physics

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. Furthermore, 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.

View Accepted Manuscript (DOE)

Research Organization:: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES); National Science Foundation (NSF); National Institutes of Health (NIH); David and Lucile Packard Foundation

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1573394

Journal Information:: Nature Chemistry, Journal Name: Nature Chemistry Journal Issue: 11 Vol. 11; ISSN 1755-4330

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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kinetics
reaction kinetics and dynamics

Temperature-jump solution X-ray scattering reveals distinct motions in a dynamic enzyme

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