期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 140, 期 26, 页码 8096-8099出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.8b04833
关键词
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资金
- National Institute of Diabetes and Digestive and Kidney Diseases
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [ZIADK029031, ZIADK075141] Funding Source: NIH RePORTER
Pressure-jump hardware permits direct observation of protein NMR spectra during a cyclically repeated protein folding process. For a two-state folding protein, the change in resonance frequency will occur nearly instantaneously when the protein clears the transition state barrier, resulting in a monoexponential change of the ensemble-averaged chemical shift. However, protein folding pathways can be more complex and contain metastable intermediates. With a pseudo-3D NMR experiment that utilizes stroboscopic observation, we measure the ensemble-averaged chemical shifts, including those of exchange-broadened intermediates, during the folding process. Such measurements for a pressure-sensitized mutant of ubiquitin show an on-pathway kinetic intermediate whose N-15 chemical shifts differ most from the natively folded protein for strands beta 5, its preceding turn, and the two strands that pair with beta 5 in the native structure.
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