Dr. Fenn will use a relatively new technique of Electrospray Mass spectrometry to study the conformation of macromolecules. Specifically, he will: (1) obtain experimental data on the non- covalent forces between amino acid molecules by using tandem mass spectrometry methods to measure the energies required to dissociate small clusters produced by ES ionization; (2) obtain experimental information on the surface area of a protein conformer ion and to investigate the hydrophobic and hydrophilic heterogeneity of that surface. Although emphasis will be placed on proteins in solution, other kinds of polymers will be considered because they may provide useful perspectives. %%% The conformation or "tertiary structure" of protein molecules determines their biological activity and so is a governing factor in many if not most of the chemical processes in living systems. Consequently, it is of vital importance to understand for any protein molecule what its active configuration is along with why and how it comes about. A hoped-for byproduct of these studies will be some insight on mechanisms by which solute ions are formed from charged droplets.

Agency
National Science Foundation (NSF)
Institute
Division of Molecular and Cellular Biosciences (MCB)
Application #
9118224
Program Officer
Kamal Shukla
Project Start
Project End
Budget Start
1992-06-15
Budget End
1994-05-31
Support Year
Fiscal Year
1991
Total Cost
$103,163
Indirect Cost
Name
Yale University
Department
Type
DUNS #
City
New Haven
State
CT
Country
United States
Zip Code
06520