ABSTRACT
The biological toxicity of high levels of breathing gases has been known for centuries, but the mechanism remains elusive. Earlier work mainly focused on the influences of dispersed gas molecules dissolved in water on biomolecules. However, recent studies confirmed the existence of aggregated gas molecules at the water-solid interface. In this paper, we have investigated the binding preference of aggregated gas molecules on proteins with molecular dynamics simulations, using nitrogen (N2) gas and the Src-homology 3 (SH3) domain as the model system. Aggregated N2 molecules were strongly bound by the active sites of the SH3 domain, which could impair the activity of the protein. In contrast, dispersed N2 molecules did not specifically interact with the SH3 domain. These observations extend our understanding of the possible toxicity of aggregates of gas molecules in the function of proteins.
Subject(s)
Gases/chemistry , Models, Chemical , Models, Molecular , Nitrogen/chemistry , src Homology Domains , src-Family Kinases/chemistry , src-Family Kinases/ultrastructure , Binding Sites , Computer Simulation , Protein Binding , Protein Conformation , Protein DenaturationABSTRACT
We have analyzed the SARS data and the effect of the control measure in HongKong, based on a spatial Monte-Carlo model (SEIR) with susceptibles, exposed(latent), infective, and recovered. The SARS data can be well fit by numerical simulations. The control measure is effective to decreasing the transmission by reducing the contact rate. The average value of the reproductive number is consistent with many of the previous models.
