
NSF Org: |
DMR Division Of Materials Research |
Recipient: |
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Initial Amendment Date: | August 21, 2002 |
Latest Amendment Date: | March 24, 2004 |
Award Number: | 0216923 |
Award Instrument: | Standard Grant |
Program Manager: |
Charles E. Bouldin
DMR Division Of Materials Research MPS Directorate for Mathematical and Physical Sciences |
Start Date: | September 1, 2002 |
End Date: | March 31, 2005 (Estimated) |
Total Intended Award Amount: | $79,100.00 |
Total Awarded Amount to Date: | $79,100.00 |
Funds Obligated to Date: |
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History of Investigator: |
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Recipient Sponsored Research Office: |
4333 BROOKLYN AVE NE SEATTLE WA US 98195-1016 (206)543-4043 |
Sponsor Congressional District: |
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Primary Place of Performance: |
4333 BROOKLYN AVE NE SEATTLE WA US 98195-1016 |
Primary Place of
Performance Congressional District: |
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Unique Entity Identifier (UEI): |
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Parent UEI: |
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NSF Program(s): | MPS DMR INSTRUMENTATION |
Primary Program Source: |
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Program Reference Code(s): |
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Program Element Code(s): |
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Award Agency Code: | 4900 |
Fund Agency Code: | 4900 |
Assistance Listing Number(s): | 47.049 |
ABSTRACT
This award from the Instrumentation for Materials Research program to the University of Washington supports the acquisition of a solid phase peptide synthesizer, and a triple channel CPMAS probe. The instrument will provide new NMR capability to the university. It will have impact in the area of molecular engineering, in characterization of biomolecules immobilized at material surfaces, in atomic level information on the structure of biopolymers adsorbed onto material surfaces and the details of protein side chain-surface interactions.
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This award from the Instrumentation for Materials Research program to the University of Washington supports the acquisition of a solid phase peptide synthesizer, and a triple channel CPMAS probe. The instrument will provide new NMR capability to the university. It will have impact in the area of molecular engineering, in characterization of biomolecules immobilized at material surfaces, in atomic level information on the structure of biopolymers adsorbed onto material surfaces and the details of protein side chain-surface interactions.
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