Student Scholar Showcase 2009

Persistent link for this collectionhttps://hdl.handle.net/11299/54848

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Browsing Student Scholar Showcase 2009 by Subject "Department of Biochemistry, Molecular Biology and Biophysics"

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    Computational Modeling of Protein Kinase A and Comparison with Nuclear Magnetic Resonance Data
    (2009-10-07) Shi, Lei; Veglia, Gianluigi
    Protein phosphorylation is fundamental in the modulation of myocardial contractility. Sarcoendoplasmic reticulum Ca2+ ATPase(SERCA) removes cytosolic Ca2+ to initiate relaxation, but the regulatory protein, phospholamban(PLN), decreases SERCA’s affinity for free Ca2+. Phosphorylation of PLN by Protein Kinase A (PKA) induces a relief of inhibition on SERCA and augments the rate of SERCA Ca2+ uptake. Here, we studied the interaction between PKA and PLN by nuclear magnetic resonance (NMR), computational docking and molecular dynamics (MD) simulations. Comparative simulations of PKA apo, binary and ternary states were performed, which provided molecular details to understand the mechanism of PKA substrate recognition.
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    EPR Analysis of Myosin Structural Dynamics
    (2009-10-07) Harris, Robert
    The structural dynamics of myosin during muscle contraction can be discerned in situ through site directed spin labeling of myosin and electron paramagnetic resonance (EPR) spectroscopy. To achieve in situ measurements, spin labeled myosin regulatory light chain (RLC) is exchanged for endogenous RLC in rabbit psoas fiber bundles. In order to ensure the structural integrity of exchanged muscle fibers, functional measurements must be done before and after exchange. After verifying function after RLC exchange, we can use EPR to measure the orientational dynamics of the RLC in a variety of states during muscle contraction.
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    The PKC Inhibitor Gö 6976 Blocks C-Type Natriuretic Peptide Activation of Guanylyl Cyclase B
    (2009-10-07) Lou, Xiaoying
    This study characterizes the effects of the widely used protein kinase C inhibitor, Gö 6976, on NPR-B guanylyl cyclase activity as a means to identify its inhibitory mechanisms.