Physics-based modeling of Hsp70-substrate binding
Molecular chaperones like DnaK help fold misfolded proteins,
but how do they distinguish well-folded, misfolded, and disordered regions?
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Molecular chaperones like DnaK help fold misfolded proteins,
but how do they distinguish well-folded, misfolded, and disordered regions?
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Why do some protein ion channels like the BK channel, which are quite large ~1.2 nm diameter, have vapor rather than physical barriers?
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Hydrophobic dewetting forms a vapor barrier and closes BK Channel; what role do specific mutations play in (de-)stabilizing this delicate liquid-vapor interplay?
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Given abundant mutational data, I’m leveraging molecular and statistical modeling to predict gating voltage of the BK channel.
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Using Newton’s laws to simulate molecular motion, like these wiggling waters:
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