9733035 Kumashiro The PI will conduct modern high-resolution solid-state nuclear magnetic resonance (NMR) experiments to characterize the molecular structure of insoluble elastin. Initially, secondary structural elements and the crosslinking moeities will be identified by 13C and 15N chemical shift measurements, respectively. Solid-state NMR experiments will then be used to ascertain the effect of different sample conditions, to probe the intramolecular interactions at work. In addition, elastin from normal and transgenic mice will be studied. The differences in NMR spectra will be indicative of the relationships between molecular structure and normal physiological function. Finally, model peptide systems related to elastin will be studied. Insoluble elastin is responsible for the elasticity in physiological structures in mammals, like blood vessels, ligaments, and skin. However, a fundamental understanding of the molecular basis of elasticity is weak, due to the lack of high-resolution structural data that is presently available. This work will focus on the elucidation of structural information on normal and defective elastin, as well as the peptides thought to be model systems for this protein. The data gathered on these systems will then be used to gain insight into the structure-property relationships of elastin. This research is highly interdisciplinary, drawing on topics as diverse as solid-state NMR to molecular biology; with this philosophy in mind, a modern learning environment for graduate and undergraduate students, both in the classroom and in the laboratory, will be provided.
