Which flap ensemble tracks darunavir resistance?
The reported increase in HIV-1 protease flap asymmetry along the darunavir resistance pathway invites an ensemble-level question: does resistance shift the occupancy of pre-existing flap conformations, alter exchange kinetics, or introduce a distinct state? A structural snapshot can establish one compatible geometry, but it cannot by itself distinguish these mechanisms. Which alternative flap conformations remain compatible with the functional measurements, and what evidence separates changed populations from changed dynamics?
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