期刊
ISRAEL JOURNAL OF CHEMISTRY
卷 57, 期 5, 页码 403-412出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/ijch.201600119
关键词
specific ion interactions; molecular dynamics simulations
资金
- Swedish National Infrastructure for Computing (SNIC) at the centre for scientific and technical computing at Lund University (Lunarc) [SNIC 2015/1-226]
- PDC Center for High Performance Computing at the KTH Royal Institute of Technology [SNIC 2016/1-222]
- PRID
Specific interactions that depend on the nature of electrolytes are observed when proteins and other molecules are studied by potentiometric, spectroscopic and theoretical methods at high salt concentrations. More recently, it became clear that such interactions may also be observed in solutions that can be described by the Debye-Huckel theory, i.e., at physiological (0.1moldm(-3)) and lower concentrations. We carried out molecular dynamics simulations of bovine serum albumin in physiological solutions at T=300 and 350K. Analysis of the simulations revealed some differences between LiCl solutions and those of NaCl and KCl. The binding of Li+ ions to the protein was associated with a negative free energy of interaction whereas much fewer Na+ and K+ ions were associated with the protein surface. Interestingly, unlike other proteins BSA does not show a preference to Na+ over K+. Quantum chemical calculations identified a significant contribution from polarisation to the hydration of Li+ and (to a lesser degree) Na+, which may indicate that polarisable force-fields will provide more accurate results for such systems.
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