Product release from human lysozyme is mediated by an intermediate state with transient weak interactions between the product and enzyme.

A spectroscopic analysis of the sarco(endo)plasmic reticulum Ca²⁺-ATPase (SERCA)-phospholamban membrane complex reveals the importance of the relative transmembrane orientation for inhibition or activation of the ATPase.

Diverse biophysical properties of β1 and β3 integrin transmembrane and cytoplasmic domains result in distinct mechanisms of integrin activation and function.

The intermediate state conformation of the human KCNQ1 potassium channel voltage sensor domain was determined, validated, and shown to be conductive under physiological conditions.

The mechanism of substrate binding cooperativity in human thymidylate synthase does not derive from millisecond dynamic interconversion between active and inactive conformations in solution, but instead results primarily from differential changes in faster side-chain motions (conformational entropy), facilitated by a disordered N-terminus.

The cysteine pair oxidation state in nDsbD acts as a ‘switch’ controlling the presence or absence of frustration in the active-site and determining the dynamic behavior of the cap loop.

Structural and biochemical analysis reveals that two intrinsically disordered domains of the transcription factor FoxM1 co-fold to form an autoinhibited conformation, which is disrupted by a specific activating phosphorylation event.

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.

Interactions in protein complexes can be predicted from evolutionary information from genomic sequences.

Ultrasonic neurostimulation in humans can manipulate response inhibition related behavior and neural activity.