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Speaker Dr Matthew Gage, Associate Professor, Department of Chemistry, University of Massachusetts Lowell
Title Deciphering the Role of Titin’s Immunoglobulin Domains
Host Mark Pfuhl
Abstract Muscle is a finely tuned organ that integrates a series of molecular motors to generate the force necessary for controlled movement, as well as involuntary processes such as breathing and our heart beating. All of these interactions have to work correctly to have proper muscle function so understanding the molecular details of the protein-protein interactions involving muscle proteins is fundamentally important. One of the often-overlooked muscle proteins is titin, which is the third contractile filament in the sarcomere. Titin spans half of the sarcomere and is generally associated with passive tension in muscle. However, recent work by the Gage lab, as well as others, has demonstrated that this protein also plays a role in active contraction as well. One of the aspects of titin that has been debated over the years is the role of the immunoglobulin domains. Initially, it was thought that the force required to unfold an immunoglobulin domain was too large to be physiologically relevant but recent studies have demonstrated that refolding of Ig domains could be contribute to the active force produced by a muscle. The Gage lab has been characterizing the stability of a series of the Ig domains in the I-band of titin to begin to decipher how varying stability might impact the biological function of these domains.