Femtosecond laser pulses at 270nm, the Ti:sapphire 3rd harmonic, are utilized to break the S-S bond in small helix bundles that are constrained to be non-helical as a result of the disulfide bridge. The resulting processes involve helix formation and geminate recombination of the sulfhydryl radicals. Both are interesting since they are controlled by the fluctuations of the protein atoms. This project involves quite the new technology of ultraviolet pumping and infrared probing of protein dynamics. A major technical goal of this work is to control the excitation processes that occur when water (or D2O) are irradiated with intense UV pulses. The two photon absorption leads to the efficient formation of solvated electrons which interfere with the methods of probing structure changes in the visible and near IR. Experiments are now underway to probe formation of helix in both water and ?-helix promoting solvents, such as trifluoroethanol (TFE).

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001348-17
Application #
6281045
Study Section
Project Start
1998-08-01
Project End
1999-07-31
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
17
Fiscal Year
1998
Total Cost
Indirect Cost
Name
University of Pennsylvania
Department
Type
DUNS #
042250712
City
Philadelphia
State
PA
Country
United States
Zip Code
19104
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