The resurrection of ancient ancestral intrinsically disordered proteins reveals the evolution of a protein-protein interaction in molecular detail.

The Mg²⁺-channel CorA explores a wide conformational landscape of non-conducting states irrespective of bound Mg²⁺, but only in abscence of Mg²⁺, conducting states become accessible due to increased backbone dynamics.

A multidisciplinary study reveals the reaction mechanism and transition state of adenosine-N⁶ methyl transfer catalyzed by human METTL3-14, deepening our insight into RNA methyltransferases and paving the way for similar studies on related enzymes.

Extensive molecular dynamics simulations enhanced by advanced sampling techniques give a detailed view of p38α canonical activation mechanism, which reveals novel key electrostatic interactions that are put in context of existing experimental data.

Molecular simulations can capture key aspects of the conformational exchange in a protein.

A combination of NMR, fluorescence, and molecular dynamics simulations reveals the recognition mechanism for the intrinsically disordered regulator of protein kinase A, highlighting the enzyme's nuclear export process.

The physical interaction network encoded in the multi-domain protein native structure handles the trade-off between the fast, stable folding and the efficient, reliable function.

Structure and simulations reveal SARS-CoV-2 NSP10 is more resistant to genetic variations than other SARS-CoV-2 NSPs and that the presence of mutations conserves structural and dynamic changes in NSP10.

Formins slow elongation of actin filament by either sterically blocking the addition of actin subunits or flattening the helical twist of the filament end.

Novel evidence on the molecular determinants of the dual function, anion permeation and substrate transport, of excitatory amino acid transporters opens avenues toward illuminating how these transporters regulate synaptic function and contribute to neurological conditions.