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Acquisition of an Analytical Ultracentrifuge for Use in Biochemistry, Structural Biology and Polymer Science

Project: Research

Project Details

Description

A grant has been awarded to the State University of New York at Stony Brook under the direction of Dr. Raleigh for the acquisition of an analytical ultracentrifuge. The analytical ultracentrifuge was first developed more than 50 years ago and its invention lead to a Nobel Prize. Since that time it has evolved from a custom made piece of specialized apparatus to an essential everyday tool for the investigation of basic biochemistry and chemistry. Analytical ultracentrifugation is the method of choice for studying the properties of large molecules that associate in solution. It is applicable to biological and non-biological systems and it is now an important research tool in biochemistry, structural biology and polymer science. The ranges of applications of this technique are immense and are rapidly increasing. Acquisition of an analytical ultracentrifuge will complement major ongoing initiatives in polymer science and in structural biology and biochemistry at SUNY Stony Brook. Ten investigators representing five academic departments at SUNY Stony Brook will conduct basic research projects. Their research interests span the range from the development of new materials, to biology, polymer chemistry, enzyme mechanisms, protein dynamics and folding, and viral assembly. Together they supervise more than 90 researchers. Professor Chu will use the instrument in his investigations of novel vesicle structures and surfactants formed by modified fullerenes. These new materials have a range of potential applications including delivery agents. Professor Kisker will use the ultracentrifugation in her studies of DNA repair while Professor de Los Santos will make use of the instrument in his studies of damaged DNA. DNA repair is essential for maintaining the correct genetic information. Mutations are the primary cause of hereditary diseases, as well as cancer, and may also be involved in aging. Professors' London and Smith will investigate fundamental issues in membrane protein structure and folding and the ultracentrifuge will play an important role in their work. It is estimated that 30 % of all proteins are membrane proteins but very little is known about their structure and folding despite the fact that they play a central role in many important biological processes. Professor Raleigh will use the instrument in his studies of the process of protein folding. The protein-folding problem refers to the mechanism by which an initially unfolded protein achieves its final functional structure. It has long been known that the linear sequence of aminoacids dictates the final folded structure of proteins but the rules that govern this key assembly process are still not understood. Professor Sampson will use the instrument in her studies of the important enzyme cholesterol oxidase, which is used as a cholesterol sensor. Professor Sampson and Professor Tonge will make use of the instrument in their basic studies of enzyme functions while the laboratory of Professor Scarlata will apply the instrument to studies of viral assembly. Professor Schindelin will use the ultracentrifuge in his studies of the proteins involved in the biosynthesis of critical molybdenum cofactors. The consortium of investigators who will make use of the analytical ultracentrifuge study fundamental problems in biology, biochemistry and polymer chemistry. Many biologically important molecules as well as many man made macromolecules work in tandem with closely associated partners. Understanding the detailed nature of these interactions is key to understanding these complex systems. An analytical ultracentrifuge is required for these studies. Examples taken from work at SUNY Stony Brook include studies of critical proteins involved in the repair of damaged genetic material, the assembly of viruses, the behavior of novel new materials made from C60 ("buckyball" derivatives), and studies of the fundamental processes by which proteins acquire their biologically active state. The instrument will also greatly enhance the infrastructure for training graduate students at SUNY Stony Brook and will also benefit researchers at nearby Brookhaven National Laboratory
StatusFinished
Effective start/end date06/1/0205/31/05

Funding

  • National Science Foundation: $223,115.00

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