Original paper
Molecular dynamics study on mobility and dipole ordering of solvent around proteins: effects of periodic-box size and protein charge
Abstract
Molecular dynamics simulations of a DNA-binding protein in charged and neutral states were done with periodic boundary boxes of different size (the distance from the protein surface to the box boundary is 6–12 Å). The protein conformation in the neutral state was stable even in the smallest box. The solvent self-diffusion coefficient reached a plateau for protein–water distances greater than 10 Å. Long-range solvent-orientational ordering, which...
Paper Details
Title
Molecular dynamics study on mobility and dipole ordering of solvent around proteins: effects of periodic-box size and protein charge
Published Date
Jun 1, 1999
Journal
Volume
306
Issue
5-6
Pages
395 - 401
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Notes
History