Author

Andrew L. Lee

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Open access Aug 2026

Dynamic view of an allosteric intermediate in a positively cooperative dimer

Positive cooperativity in ligand binding is a hallmark of allosteric oligomers, yet how the first binding event enhances the second remains obscure, because the pivotal singly-bound intermediate (lig₁) is thermodynamically disfavored and rarely accumulates. Distinguishing concerted (MWC) from sequential (KNF) mechanism...

P. J. Sapienza, T. Mileur, M. S. Khan et al. · bioRxiv · 0 citations

Open access Aug 2026

Incidental conformational switching in an allosteric enzyme

It is proposed that the observed T-to-R switching in CM is “incidental”, a byproduct of an evolved energy landscape that allows access to the substrate-bound pose but does not mechanistically determine affinity.

P. J. Sapienza, Darex J. Vera-Rodriguez, T. Mileur et al. · bioRxiv · 0 citations