From attaching DNA enzymes to nanotubes to simulating proteins under pressure, the work of 33 Rensselaer researchers was presented at the 231st American Chemical Society (ACS) National Meeting March 26-30 in Atlanta.

Following are a few Rensselaer highlights from the meeting:

Rensselaer researchers led by Jonathan Dordick, the Howard P. Isermann ’42 Professor of Chemical and Biological Engineering at Rensselaer, and Ravi Kane, the Merck Associate Professor of Chemical and Biological Engineering at Rensselaer, presented results from work on attaching DNA enzymes to multi-walled carbon nanotubes to create hybrid materials that are highly active and stable. These DNA-nanotube hybrids might provide important opportunities as templates for nanoscale assembly and as nanoscale cellular therapeutics, they say. Rensselaer chemical and biological engineering graduate student Tae-Jin Yim made the research presentation at the meeting. The project is done in collaboration with researchers at the University of Illinois at Urbana-Champaign.

A collaborative team of Rensselaer researchers led by Curt Breneman, professor of chemistry and chemical biology, is working to identify an efficient procedure for selecting protein displacers, which have shown great potential for the purification of proteins from complex mixtures. Protein purification methods are widely used in drug discovery and proteomics, but the selection of displacers is still mostly driven by trial-and-error and is largely dependent on the knowledge of an expert, according to the Rensselaer team. The researchers are working to refine a new computational procedure that will quickly predict novel selective displacers from available commercial chemical catalogs using a high-throughput screening method.

The surfaces of proteins, DNA, and other biomolecules interact with water to form the very basis of life. In water-based solutions, proteins instinctively fold into unique three-dimensional structures, which do much of the work in the body. The ability of proteins to function depends on their ability to fold and vibrate sufficiently in their folded state, and misfolded proteins are implicated in diseases such as Alzheimer’s and Parkinson’s. Rensselaer and University of Texas at Austin researchers presented a computer simulation study at the meeting that demonstrates the role of hydrostatic pressure of water in protein structure and function. Led by Shekhar Garde, associate professor of chemical and biological engineering at Rensselaer, research contributors included Rensselaer chemical and biological engineering graduate students Sowmianarayanan Rajamani and Manoj Athawale.

For more information about the meeting, including the full technical program, visit http://chemistry.org/meetings/atlanta2006.

Published April 3, 2006