Solute transport in orthorhombic lysozyme crystals: a molecular simulation study |
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Authors: | Kourosh Malek |
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Institution: | (1) Department of Chemistry, University of Tehran, P.O. Box 14155-6455, Tehran, Iran |
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Abstract: | Long-time equilibrium molecular dynamics simulations were performed to study the passage of a substrate, l-arabinose, through nanopores of orthorhombic hen egg white lysozyme crystals. Cross-linked protein crystals (CLPC), as novel
biological nanoporous media, consist of an extensive regular matrix of chiral solvent-filled nanopores via which ions and
solutes, e.g. sugars and amino acids, travel in and out. We studied the diffusive motion of arabinose inside protein channels.
The computed diffusion coefficients within the crystal were orders of magnitudes lower relative to the diffusion coefficient
of the solute in water. This study is valuable for understanding the nature of solute–protein interactions and transport phenomena
in CLPCs and provides an understanding of biocatalytic and bioseparation processes using CLPC. |
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Keywords: | Diffusion l-arabinose" target="_blank">l-arabinose Lysozyme Molecular dynamics Protein crystal |
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