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Expanding the range of nature's catalysts for industrial applications
Date:1/30/2014

Troy, N.Y. To make paper, manufacturers must break down cellulose (chunks of wood pulp), a process that currently requires large amounts of energy and toxic chemicals like chlorine. Nature performs the same task using enzymes, non-toxic biodegradable proteins that accelerate chemical reactions using far less energy. The catch is that the enzymes required for the job, in this case xylanases, don't hold up to the high temperatures of the manufacturing process. This is only one of many examples of how the limitations of enzymes hamper the development of elegant solutions in the manufacture of everything from medicine to detergents.

"So the question is: can we improve on nature?" said George Makhatadze, a chaired professor in the Biocomputation and Bioinformatics research constellation, professor of biological sciences, and member of the Center for Biotechnology and Interdisciplinary Studies (CBIS) at Rensselaer Polytechnic Institute. "Can we take an existing protein and, using computation, redesign it to withstand higher temperatures?"

Makhatadze designs "custom proteins," and is an expert in the critical interaction between electrical charges on the surface of proteins. Within the School of Science, Makhatadze's research is part of an interdisciplinary theme of modeling, analysis, and simulation. His research is also part of a CBIS research focus on protein engineering. In a 2009 edition of the Proceedings of the National Academy of Science (PNAS), his lab presented a computer model that enhances protein thermostability, while retaining full enzymatic activity. Now, with the support of a five-year, $1.7 million National Science Foundation grant, Makhatadze will investigate the speed of protein folding.

Enzymes are composed of long strings of amino acids. As the string is assembled, electrostatic forces along its length interact, causing it to twist and turn, and ultimately fold into a stable three-dimensional shape. The enzyme function
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Contact: Mary Martialay
martim12@rpi.edu
Rensselaer Polytechnic Institute
Source:Eurekalert

Page: 1 2 3

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