Single-molecule insights into SAM-I riboswitch ligand binding using scaled magnetic force spectroscopy with comparison to conventional biophysical methods
Single-molecule force spectroscopy reveals distinct conformational dynamics induced by SAM versus SAH in SAM-I riboswitches, highlighting divergent RNA stabilization mechanisms.
Key Points
Determine how SAM and SAH binding differentially affect the conformational dynamics and mechanical stability of the SAM-I riboswitch.
Applied scaled magnetic force spectroscopy to subject SAM-I riboswitch RNA to constant forces across extended periods.
Tracked and compared the conformational dynamics of RNA complexes formed with SAM versus SAH ligands.
Application of constant mechanical force demonstrates distinct conformational dynamics in SAM-I riboswitches upon SAM binding compared to SAH binding.
Ligand-dependent mechanical responses indicate fundamentally different stabilization mechanisms between SAM and SAH interactions.