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- W2034262217 abstract "We have used site-directed spin labeling and pulsed dipolar electron-electron paramagnetic resonance (DEER) to resolve the structure and dynamics of flexible and disordered regions of myosin binding protein-C (MyBP-C)'s cardiac isoform, with implications for the pathophysiology of hypertrophic cardiomyopathy (HCM). N-terminal domains of cMyBP-C contain binding domains for several interaction partners in the myofilament, including myosin heavy chain subfragment 2 (S2) and actin. We engineered pairs of labeling sites in protein fragments of mouse cMyBP-C to measure with high resolution distance and disorder between (1) domains C0 and C1, flanking the flexible Pro/Ala-rich linker, and between (2) domains C1 and C2, flanking the partially disordered phosphorylation motif, using DEER. Changes in distance and disorder were assessed for double-Cys mutant cMyBP-C's free in solution and when bound to myosin S2 or actin, with or without cMyBP-C phosphorylation by protein kinase A (PKA). Understanding conformational transitions in the flexible and dynamic portions of cMyBP-C upon actin-myosin binding and phosphorylation provide new molecular insight into defining its modulatory role in muscle force development. (NIH-F32 to BAC; NIH-R01 to DDT)" @default.
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- W2034262217 date "2013-01-01" @default.
- W2034262217 modified "2023-09-29" @default.
- W2034262217 title "Structural Dynamics of Actin-Myosin Bound and Unbound States of Cardiac Myosin Binding Protein-C Detected by Dipolar EPR" @default.
- W2034262217 doi "https://doi.org/10.1016/j.bpj.2012.11.1054" @default.
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