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Structural and dynamical changes in an alpha-subunit of a heterotrimeric G protein along the activation pathway.
Mechanism of the receptor-catalyzed activation of heterotrimeric G proteins.
Mapping allosteric connections from the receptor to the nucleotide-binding pocket of heterotrimeric G proteins.
Helix dipole movement and conformational variability contribute to allosteric GDP release in Galphai subunits.