The ability of proteins to guide small molecules to reaction sites and across membranes is essential to many metabolic pathways, but the process is not well understood. Now, scientists at the University of Illinois at Urbana-Champaign have shown that a globular protein with a barrel structure can direct small molecules in much the same fashion as a membrane protein.
Chemistry professor Zaida Luthey-Schulten, graduate student Rommie Amaro, and Emad Tajkhorshid, assistant director of physics research at the universitys Beckman Institute for Advanced Science and Technology, used molecular dynamics simulations to study the movement of ammonia during the biosynthesis of the amino acid histidine. A paper describing the results is to be published the week of June 9 in the Online Early Edition of the Proceedings of the National Academy of Sciences. The print version will appear at a later date.
Most living organisms are composed of a set of 20 amino acids, the so-called "building blocks of life." Each of these amino acids is produced through what can be thought of as a biological assembly line. Starting with a small part, subsequent parts are added or removed by enzymes until the final compound is formed. These final compounds become the major components of proteins and tissues.
James E. Kloeppel | UIUC
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