NSF Org:	CHE Division Of Chemistry
Recipient:	THE LELAND STANFORD JUNIOR UNIVERSITY
Initial Amendment Date:	July 9, 1990
Latest Amendment Date:	April 24, 1991
Award Number:	9018241
Award Instrument:	Standard Grant
Program Manager:	Seymour Lapporte CHE  Division Of Chemistry MPS  Directorate for Mathematical and Physical Sciences
Start Date:	September 1, 1990
End Date:	February 29, 1992 (Estimated)
Total Intended Award Amount:	$36,700.00
Total Awarded Amount to Date:	$36,700.00
Funds Obligated to Date:	FY 1990 = $32,000.00 FY 1991 = $4,700.00
History of Investigator:	John Griffin (Principal Investigator) JGRIFFIN@LELAND.Stanford.EDU
Recipient Sponsored Research Office:	Stanford University 450 JANE STANFORD WAY STANFORD CA  US  94305-2004 (650)723-2300
Sponsor Congressional District:	16
Primary Place of Performance:	DATA NOT AVAILABLE
Primary Place of Performance Congressional District:
Unique Entity Identifier (UEI):	HJD6G4D6TJY5
Parent UEI:
NSF Program(s):	CHEMISTRY FELLOWSHIPS
Primary Program Source:
Program Reference Code(s):	9251
Program Element Code(s):	198800
Award Agency Code:	4900
Fund Agency Code:	4900
Assistance Listing Number(s):	47.049

ABSTRACT

This award is made as the starter grant increment of Dr. John Griffin's Postdoctoral Fellowship in Chemistry Award in support of his research at Stanford University. The thrust of Dr. Griffin's research is the isolation, purification and characterization of enzyme and antibody catalysyts for polyene cyclization reactions. Enzymatic activity of purified cyclase will be quantified and the amino acid and gene sequence will be determined. The cyclizing acive site will be studied through affinity labelling and directed mutagenesis experiments. This should permit the design and preparation of engineered enzymes having novel substrate and/or product specificities. Heterobicyclic immunogens will be synthesized which will elicit antibodies capable of initiating, directing and terminating the cyclization of diene epoxides. Once antibody catalysts have been identified, their mechanism of action will be studied. This should lead to a better understanding of sterol biosynthesis and macromolecular catalysis and may provide useful catalysts for the synthesis of sterols.

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