Ning Ma

The paper shows that a second G protein couples with higher affinity to a GPCR dimer than the first, due to conformational stabilization by the first G protein.

This study investigates how odorant receptors regulate selectivity and antagonism through allosteric gating mechanisms using simulations and experiments.

The paper identifies subtype-specific conserved residues in G protein subtypes that modulate Gβγ coupling, showing conservation does not guarantee functional equivalence.

This study shows that frustration in the SMARCA2-VHL protein-protein interface correlates with PROTAC cooperativity, offering a framework for structure-based PROTAC design.

The paper identifies frustrated residues in GPCR:G protein interfaces and engineered degrader complexes, showing higher frustration in engineered interfaces.

BaNDyT uses Bayesian network modeling to analyze molecular dynamics trajectories, providing data-driven insights into protein function and interactions.

This study uses protein frustration analysis to identify key residues distinguishing strong from weak BRD4-Cereblon degraders.

This study shows that lipids like PIP2 and GM3 modulate the conformation of ICL3 in beta-2AR, affecting G protein coupling through membrane tilting and allosteric effects.

This study uses Bayesian network modeling to identify cooperative GPCR:G protein interactions and their allosteric effects, revealing subnetworks that contribute to G protein coupling selectivity.

The paper uses engineered odorant receptors to uncover structural principles of odor discrimination by solving cryoEM structures of consensus ORs and comparing their ligand recognition properties.

The paper determines the cryo-EM structure of mTAAR7f bound to DMCH, revealing its unique binding site and activation mechanism distinct from ORs.