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Rna helicases, which participate in nearly all aspects of rna
metabolism, utilize the energy from Atp hydrolysis to unwind rna.
The engine core of helicases is usually made of a pair of RecA-like
domains that form an Ntp binding cleft at their interface.
Changes in the chemical state of the Ntp binding cleft (binding of
the Ntp or its hydrolysis products) alter the relative positions of
the RecA-like domains and nucleic acid-binding domains, creating
structural motions that disrupt the pairing of the nucleic acid,
causing separation and unwinding.
Most Rna helicases utilize a mechanism known as canonical duplex
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