Champaign, Ill -- U.S. scientists are using custom-built spectrometers and other novel assets to better understand the form and function of certain proteins in the human body.
University of Illinois scientists said their improved capability of probing protein chemistry and structure includes the use of solid-state nuclear magnetic resonance spectroscopy, producing significant progress toward atomic-scale resolution of protein structure by solid-state NMR spectroscopy.
"In our experiments we explore couplings between atoms in proteins," said Professor Chad Rienstra, who led the research. "Our goal is to translate genomic information into high-resolution structural information and thereby be able to better understand the function of the proteins.
"With increased speed and sensitivity, we can obtain very high-resolution spectra. And, because we can resolve thousands of signals at a time -- one for each atom in the sample -- we can determine the structure of the entire protein."
Rienstra described his group's latest findings in Philadelphia this week during the national meeting of the American Chemical Society. The work was initially reported in the March 25 issue of the Proceedings of the National Academy of Sciences.
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