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Award Abstract #0216201
Acquisition of a High Field Solid State NMR Spectrometer
| NSF Org: |
CHE
Division of Chemistry
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| Initial Amendment Date: |
August 6, 2002 |
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| Latest Amendment Date: |
August 6, 2002 |
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| Award Number: |
0216201 |
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| Award Instrument: |
Standard Grant |
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| Program Manager: |
Robert L. Kuczkowski
CHE Division of Chemistry
MPS Directorate for Mathematical & Physical Sciences
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| Start Date: |
August 15, 2002 |
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| Expires: |
July 31, 2005 (Estimated) |
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| Awarded Amount to Date: |
$770000 |
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| Investigator(s): |
Gina Hoatson gina@physics.wm.edu (Principal Investigator)
Robert Vold (Co-Principal Investigator)
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| Sponsor: |
College of William and Mary
Grants & Research Admin.
Williamsburg, VA 23187 757/221-3485
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| NSF Program(s): |
MAJOR RESEARCH INSTRUMENTATION
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| Field Application(s): |
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| Program Reference Code(s): |
BIOT, AMPP, 9184, 9161
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| Program Element Code(s): |
1189
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ABSTRACT
With support from the Major Research Instrumentation (MRI) Program at NSF, and the Department of Defense, Profs. Gina Hoatson and Robert Vold at the College of William and Mary will acquire a high field (18 tesla), multinuclear solid state nuclear magnetic resonance (NMR) Spectrometer. This equipment will enable researchers to carry out studies on a) ferroelectric and piezoelectric materials; b) high performance carbon nitride films; c) technologically important conducting polymers; and d) biologically important amino acids and cyclic dipeptides.
Nuclear Magnetic Resonance (NMR) spectroscopy is the most powerful tool available to chemists for the elucidation of the structure of molecules. It is used to identify unknown substances, to characterize specific arrangements of atoms within molecules, and to study the dynamics of interactions between molecules in solution. Access to state-of-the-art NMR spectrometers is essential for carrying out frontier research. The results from these NMR studies will have an impact in a number of areas including development of wear-related coatings, ultrasonic transducers and electronic actuators, and electrochromic devices. In addition, amino acids and cyclic dipeptides are important to study because these model systems yield insight into problems of protein folding, molecular recognition and enzyme activity.
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