Douglas P. Ridge, Professor(302) 831-1197 • dougr@udel.edu • http://www.udel.edu/chem/ridge/
(b. 1944) A.B., 1968, Harvard University; Ph.D., 1972, California Institute of Technology
Recent work has shown that linkage isomers of peptides can be distinguished using collision induced decomposition. Ion molecule reactions studies have demonstrated the persistence of helical secondary structure of selected peptides on electrospray ionization, provided information on the energetics of intramolecular hydrogen bonding in amino acids, and elucidated details of the mechanisms of metabolic processes relevant to the toxicity of halogenated industrial wastes.
Investigation of the potential of electron attachment as a means of activating multiply charged peptide ions is under way. FTMS examination of protein-RNA non-covalent complexes promises to characterize bonding between the protein and RNA. Studies of metals and metal ions have led to measurement of the binding energy of NO to several metalloporphyrins including heme, and a demonstration of the application of organometallic ion-molecule reactions to the determination of the molecular weight distributions of polyolefins. Another problem of environmental interest studied recently is the complexation of potentially toxic metals with sulfides in river water. Particularly exciting is the recent demonstration that IR multiphoton dissociation, IRMPD, vibrational spectra of trapped metal clusters not otherwise observable can be obtained using FTMS and a tunable free electron laser, opening the door to structural investigations of a rich variety of reactive and interesting species.