Abstract
Molecular dynamics simulations of a coarse-grained, embedded-charge model of lysozyme aqueous solutions are compared with small-angle neutron scattering experiments. Measures concern different solutions with a 10% by weight protein concentration and an increasing pH in the range 2–6. The model is based on a soft-core modification of the original Carlsson–Malmsten–Linse model, where in particular all residues carrying an appreciable amount of residual charge, as a function of the pH, are explicitly taken into account in the overall macromolecular interaction. Simulations reproduce qualitatively the experimental trend of the structure factor such as, in particular, the observed change from a low-pH regime, dominated by repulsive interactions, to behaviour mainly determined by attractive forces, at higher pH. Possible improvements of the model, towards a better reproduction of the structural properties of the real solution, are proposed.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
