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The RNA's structure facilitates the helicase's movement along its sequence. G-patch (gp) factors stimulate Prp43's cellular ATPase and RNA unwinding activity, which is inherently weak. The exact procedure by which Prp43 performs RNA loading and how it is influenced by substrates such as ATP, RNA, and G-patch partners, remains unclear. To examine the real-time conformational fluctuations of the RNA binding channel within Prp43, single-molecule (sm) FRET reporters were engineered from Prp43 in Chaetomium thermophilum. Evidence sugge
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