January 18, 2007
Science Paper Focuses on Role of Cysteines in Proteins
LINCOLN, Neb. — A team of scientists led by University of Nebraska-Lincoln biochemist Vadim Gladyshev has developed a new way to rapidly identify amino acids in proteins that have redox function. The work is published in the current issue of Science magazine.
The process developed by Gladyshev and Dmitri Fomenko, a research assistant professor in Gladyshev's laboratory, focuses on cysteines, amino acids found in most proteins. In some proteins, cysteines have no critical function, while in others they play roles such as binding metals, regulating certain protein functions, or targeting proteins to a particular location in cells. In still other proteins, cysteines are key players in redox regulation, which is a basic biological process used by all organisms.
The team's work, which used Prairiefire, UNL's renowned supercomputer, developed a simple, accurate way to determine which cysteines are redox active. Following this bioinformatics procedure, the researchers then verified their technique by characterizing a protein involved in arsenic detoxification, one of many proteins the team has found to contain a redox cysteine.
Cysteine appears to be unique among other amino acids found in proteins in that it is amenable to this approach, which provides large-scale, highly selective prediction independent of protein type or organism from which the protein is derived.
Other members of the team who coauthored the article are David Thomas and Blakely Adair of the Environmental Protection Agency, and Weibing Xing of the University of North Carolina.
1/18/07-DM
Vadim N. Gladyshev - Ph.D.
Biochemistry
Professor
(402) 472-4948
Dan Moser IANR News & Photography Coordinator (402) 472-3007
Department: Biochemistry
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