BioEmu2 simulations show ligand-triggered conformational shifts in maltose binding protein

FrankNoeBerlin · x · 2026-11-10

• Douglas Glin shared first results from experimenting with BioEmu2, focusing on maltose binding protein (MBP), which captures maltose in the bacterial periplasm. Its native ligand maltotriose can displace the NMR reporter α-gluco-2-fluoromaltose from MBP, while cellobiose cannot.
• The simulations suggest both ligands trigger a conformational change, whereas the apo form mostly stays where it starts.
• The results illustrate how generative biomolecular dynamics models can be used to probe ligand-induced conformational changes.

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