Langevin dynamics of proteins at constant $p\mathrm{H}$

An application of the Langevin dynamics algorithm for simulation of protein conformational equilibria at constant $p\mathrm{H}$ is presented. The algorithm is used to compute average protonation of titratable groups in ovomucoid third domain, as functions of $p\mathrm{H},$ resulting in data, basically equivalent to the $p\mathrm{H}$ dependencies of chemical shifts obtained from multidimensional nuclear magnetic resonance (NMR) spectroscopy, for the protein titratable residues. The $p{\mathrm{K}}_a$ values obtained from the simulation are in reasonable agreement with experimental data. Possible improvements of this methodology, using achievements from other fields of mesoscopic biomolecular simulations, are also discussed.