MRI: Acquisition of a High Pressure Stopped-Flow Instrument for Studying Biological Systems under Extreme Conditions

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An award is made to Rensselaer Polytechnic Institute to support the purchase of high-pressure stopped flow (HPSF) spectrophotometer/fluorimeter system. The instrument is the first of its kind in the US and will be housed in the RPI Analytical Biochemistry Core Facility. This will ensure that the unique cutting-edge capabilities of the instrument will be accessible to undergraduate students, graduate students, and postdoctoral fellows, not only at RPI but also to a broader community in the NY Capital Region and beyond. A number of laboratories will use the instrument to address questions of basic biochemistry, biology and evolutionary adaptations to extreme environments. The instrument will also be used in a number of hands-on workshops that will include undergraduate and graduate students. The participation in these workshops will be extended to the laboratories from NSF-supported Research Coordination Network on Extreme Biophysics (RCN-EB). In addition, the research that is enabled by this instrument will be incorporated in community outreach programs to encourage students into STEM fields and reaches out to talented underrepresented minorities and young women in the NY Capital Region. Hydrostatic pressure is an important environmental variable that plays an essential role in biological adaptation for many extremophilic organisms that inhabit the depth of the oceans and subsurface crusts. The HPSF instrument will support research activities of a group of investigators interested in understanding the molecular details of the effects of high hydrostatic pressure on the biological function and functional dynamics of biological macromolecules. The ability to experimentally monitor enzyme kinetics as a function of temperature and pressure using the HPSF instrument is critical for understanding of how hydrostatic pressure modulates the activity of the enzymes. This in turn will lead to a better understanding of adaptation of organisms to extreme pressures. High-hydrostatic pressure can also influence the energy landscape for protein folding. High-energy states of proteins are implicated in catalysis, binding, aggregation, allostery, and folding, thus connecting the enzymatic function with their dynamic properties. The results of these research efforts will be disseminated through active participation of students and faculty at scientific conferences, symposia and workshops, through peer-reviewed publications and public outreach presentations.This award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.