Ct. Reimann et al., PROTEINS IN-VACUO - DENATURATION OF HIGHLY-CHARGED LYSOZYME STUDIED BY MOLECULAR-DYNAMICS SIMULATIONS, JOURNAL OF PHYSICAL CHEMISTRY B, 102(46), 1998, pp. 9344-9352
Molecular dynamics (MD) simulations have been employed to address the
structural changes of lysozyme (LYZ) in vacuo driven by Coulomb forces
associated with multiple protonation, as occurs in electrospray ioniz
ation. Some general features which emerged from this MD study are that
sufficiently high charge states drove significant unfolding and resha
ping of the tertiary structure, while domain and secondary structures
survived to some extent. Generally, higher charge was required to effe
ct denaturation in comparison with experimental observations. Other ph
ysical factors not presently included in the model, viz., high interna
l energy, may be required to reduce the barrier for driving the unfold
ing process.