University of Connecticut |
Polymer Program SeminarSolid-state NMR Spectroscopy of Elastin and its Mimetics: Insights into a Resilient Biological Elastomer Monday, February 12, 2007 11:00 am , IMS Room 20 Elasticity in vertebrate tissue originates from /elastin/, a crosslinked, amorphous protein with a unique composition. Until recently, very little high-resolution structural information was available for elastin, due largely to its insolubility and predominantly hydrophobic composition. As a result, the models for elastin's elasticity are controversial. Solid-state NMR spectroscopy (ssNMR) is a powerful tool that has been utilized to determine the structural and dynamic features of peptides and other biopolymers, particularly those for which the solid state is the most biologically relevant. The growth of applications for ssNMR has been exponential over the last two decades, and elastin appears to be an ideal candidate for many of these approaches. In this talk, studies of elastin and numerous mimetics are described. The utility of fairly straightforward 1D measurements, based largely on C-13 CPMAS NMR and related techniques, is highlighted. In addition, a new approach for the production of isotopically-enriched nativelike elastin is introduced. These results and the implications for models of elastin's structure-function relationships will be discussed.
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