On the similarity of properties in solution or in the crystalline state: A molecular dynamics study of hen lysozyme |
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Authors: | U Stocker K Spiegel WF van Gunsteren |
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Institution: | (1) Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, CH-8092 Zürich, Switzerland;(2) Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, CH-8092 Zürich, Switzerland;(3) Laboratory of Physical Chemistry, Swiss Federal Institute of Technology, CH-8092 Zürich, Switzerland |
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Abstract: | As protein crystals generally possess a high water content, it is assumed that the behaviour of a protein in solution and in crystal environment is very similar. This assumption can be investigated by molecular dynamics (MD) simulation of proteins in the different environments. Two 2ns simulations of hen egg white lysozyme (HEWL) in crystal and solution environment are compared to one another and to experimental data derived from both X-ray and NMR experiments, such as crystallographic B-factors, NOE atom–atom distance bounds, 3JH N -coupling constants, and 1H-15N bond vector order parameters. Both MD simulations give very similar results. The crystal simulation reproduces X-ray and NMR data slightly better than the solution simulation. |
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Keywords: | lysozyme molecular dynamics simulation NMR solution structure protein dynamics X-ray crystal structure |
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