NMR Studies of Elastin Structure and Dynamics

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The objective of this project is to provide new insight into biological elasticity and other properties of proteins that are tied to hydrophobicity. The uniquely resilient and elastic properties of skin and blood vessels have been traced to elastin, the principal protein component of the fibers that comprise a large portion of these tissues. Elastin is comprised primarily of long hydrophobic chains interspersed with alanine-rich crosslinking regions. The very nature of this protein precludes the use of classic high-resolution structural tools, such as crystallography and solution NMR spectroscopy. With the prior support from the NSF's CAREER program, the PI used solid-state NMR in conjunction with a novel approach in isotopic labeling to elucidate new structural information on this complex biopolymer. In this project, the structural and dynamic characterization of elastin and elastin peptides will be expanded. The major focus is the structural characterization of isotopically-enriched insoluble elastin from cell culture using solid-state NMR spectroscopy. These studies will be complemented by analogous work on elastin peptides from synthesis and bacterial expression. Finally, investigations of the dynamics in these systems will be pursued. All results will be integrated to provide a comprehensive picture for biological elasticity. The research will involve students at all levels - undergraduate, graduate, and postdoctoral. The research training experience provided herein is cross-disciplinary, exposing students to a range of techniques and expertise, particularly as the project involves several collaborators in elastin biochemistry and matrix biology.