L. Swint-Kruse

The study shows that the intrinsically disordered activation domain of CIITA is tuneable by single amino acid substitutions, challenging the acidic exposure model and suggesting variability in IDR tuneability.

The paper identifies multiplex rheostat positions in LacI that modulate multiple functional parameters and shows they overlap with allosteric regions, suggesting complex biophysical effects.

The paper identifies a rheostat position in NTCP where substitutions produce varied functional effects, showing substrate-dependent transport changes and structural stability variations.

The paper shows that substitutions at nonconserved positions in the LacI protein alter DNA binding by re-wiring long-range dynamic interactions.

The paper identifies biochemically neutral positions in human liver pyruvate kinase by analyzing evolutionary patterns and functional outcomes of amino acid substitutions.

The paper evaluates how distant mutations affect allosteric coupling between effector binding sites in pyruvate kinase, finding that distant positions can fully tune allosteric coupling.