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Speaker: Dr Neil Kad, School of Biosciences, University of Kent
Host: Elizabeth Ehler
During muscle contraction actin provides a surface for myosin to pull against. However, exposure of actin's surface is not passive and requires substantial levels of control to prevent spurious contractions. This is achieved by the control proteins tropomyosin and troponin, which respond to calcium to reveal myosin binding sites. Such a simple model is confounded by the intervention of other proteins such as myosin binding protein-C (MyBP-C); this enigmatic protein interacts with both myosin and actin. In this talk I will discuss our findings using single molecule imaging methods to investigate how myosin, calcium and MyBP-C cooperate to finely tune the contractility of muscle. When this fine-tuning is interrupted serious, long-term conditions such as cardiomyopathies can result, highlighting the importance of a complete dynamic, molecular understanding of contraction.
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