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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Molecular dynamics simulation of E. coli ribonuclease H1 in solution: correlation with NMR and X-ray data and insights into biological function.

A 500 ps molecular dynamics simulation of Escherichia coli RNase H1 in the presence of explicit water molecules has been carried out to aid in the interpretation of NMR N-H backbone model free parameters and X-ray B-factor values of the free enzyme. Both experimental techniques have revealed unusual structural and dynamic features of the protein. Atomic fluctuations (B-factors) and re-orientational motions of the backbone heteronuclear bonds (order parameters) computed from the simulation are compared with results obtained from experiments. Qualitative agreement is obtained between the computed and X-ray B-factors, whereas the agreement between the computed and NMR generalized order parameters is as good as quantitative for most residues. Reasons for significant discrepancies, the physical basis and the plausible biological consequences of the observed protein dynamics are discussed.[1]


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