Towards a Fuller Understanding of Salt-Bridges in Proteins
Recent studies have cast doubt on the validity of salt bridge forcefields widely used in molecular dynamics. D4C remains one of the few instruments that can structurally examine this problem. The goal of this experiment is to acquire data that can be used to assess the validity of the protein force fields for salt bridges. This will be done by measuring first order neutron scattering differences on various aqueous acetate solutions. Isotopic substitution (H/D) will be performed on the acetate ions, with this ion being used as a proxy for the anionic part of the salt bridge. Similar experiments will the be performed with different counterions (chosen as proxies for the cation part of the salt bridge). This data, combined with molecular dynamics simulations of the same systems will allow for an accurate assessment of the validity of the protein forcefields and allow greater structural insight into these systems.
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MASON Philip; DEMPSEY C; Henry E. Fischer; HLADILKOVA Jana; JUNGWIRTH Pavel and TIMR Stepan. (2014). Towards a Fuller Understanding of Salt-Bridges in Proteins. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-807
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