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Bipasha Barua

As seen in: BioRxiv
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Articles

A myosin hypertrophic cardiomyopathy mutation disrupts the super-relaxed state and boosts contractility by enhanced actin attachment

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By Robert C. Cail, Bipasha Barua, Faviolla A. Báez-Cruz, Donald Winkelmann
| BioRxiv
Abstract Hypertrophic cardiomyopathy (HCM) is a leading cause of cardiac failure among individuals under 35. Many genetic mutations that cause HCM enhance ventricular systolic function, suggesting that these HCM mutations are hypercontractile. Among the most common causes of HCM are mutations in the gene MYH7, which encodes for beta-cardiac myosin, the principal human ventricular myosin.
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S2Tag, a novel affinity tag for the capture and immobilization of coiled-coil proteins: application to the study of human β-cardiac myosin

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By Bipasha Barua, Robert C. Cail, Yale E. Goldman, E. Michael Ostap
| BioRxiv
Abstract Single molecule and ensemble motility assays are powerful tools for investigating myosin activity. A key requirement for the quality and reproducibility of the data obtained with these methods is the mode of attachment of myosin to assay surfaces. We previously characterized the ability of a monoclonal antibody (10F12.3) to tether skeletal muscle myosin to nitrocellulose coated glass.
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Investigating the effects of tropomyosin mutations on its flexibility and interactions with filamentous actin using molecular dynamics simulation

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By Wenjun Zheng, Bipasha Barua
| Journal of Banking Regulation Verified
Tropomyosin (Tpm) is a two-chained ?-helical coiled-coil protein that binds to filamentous actin (F-actin), and regulates its interactions with myosin by occupying three average positions on F-actin (blocked, closed, and open). Mutations in the Tpm are linked to heart diseases including hypertrophic cardiomyopathy (HCM) and dilated cardiomyopathy (DCM).
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