We are interested in the secondary structure of short peptides in aqueous solutions. Previous studies within our group have shown that a series of D-Pro containing 16-mers adopt monomeric ?-hairpin conformations in aqueous solution, while their all-L stereoisomers do not. We plan to probe the fundamental requirements for ?-hairpin formation in water. The first objective will be to determine the minimum number of residues necessary for a stable ?-hairpin. The second goal will be to perform structure-activity studies with the aim of learning how specific residues and interresidue interactions contribute to b-hairpin stability. Peptides designed to contain multiple hairpins will also be analyzed. Our group has previously identified ?-hairpin formation in both organic and aqueous media using NMR techniques. COSY and TOCSY experiments facilitate peak assignments, while NOESY and/or ROESY experiments provide information regarding the three-dimensional solution structure. Additional experimental techniques for characterization of synthesized peptides will include circular dichroism and IR studies.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
3P41RR002301-15S1
Application #
6120939
Study Section
Project Start
1999-03-01
Project End
2000-02-29
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
15
Fiscal Year
1999
Total Cost
Indirect Cost
Name
University of Wisconsin Madison
Department
Type
DUNS #
161202122
City
Madison
State
WI
Country
United States
Zip Code
53715
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