Titration properties and determinants in intrinsically disordered proteins.

Rizzuti B., Cozza C., Neira J.L.
  Giovedì 14/09   09:00 - 11:30   Aula A209   V - Biofisica e fisica medica
Charged amino acids are highly abundant and have a crucial function in intrinsically disordered proteins (IDPs). The $p{K}_{a}$ values of titratable protein residues were investigated to clarify the molecular determinants of electrostatic interactions in two IDPs, namely NUPR1 and IF7. Solution structures obtained through molecular dynamics simulations were experimentally validated and used to obtain theoretical estimates of the titration midpoints, which were compared with the values obtained for acidic residues by using NMR spectroscopy. The results suggest that local interactions can play a variable role in determining the electrostatic features of IDPs, whereas long-range charge contributions are of lesser importance.