Picture offshore wind farm

Open Access research that is improving renewable energy technology...

Strathprints makes available scholarly Open Access content by researchers across the departments of Mechanical & Aerospace Engineering (MAE), Electronic & Electrical Engineering (EEE), and Naval Architecture, Ocean & Marine Engineering (NAOME), all of which are leading research into aspects of wind energy, the control of wind turbines and wind farms.

Researchers at EEE are examining the dynamic analysis of turbines, their modelling and simulation, control system design and their optimisation, along with resource assessment and condition monitoring issues. The Energy Systems Research Unit (ESRU) within MAE is producing research to achieve significant levels of energy efficiency using new and renewable energy systems. Meanwhile, researchers at NAOME are supporting the development of offshore wind, wave and tidal-current energy to assist in the provision of diverse energy sources and economic growth in the renewable energy sector.

Explore Open Access research by EEE, MAE and NAOME on renewable energy technologies. Or explore all of Strathclyde's Open Access research...

Mechanism of hen egg white lysozyme adsorption on a charged solid surface

Kubiak-Ossowska, Karina and Mulheran, Paul A. (2010) Mechanism of hen egg white lysozyme adsorption on a charged solid surface. Langmuir, 26 (20). pp. 15954-15965. ISSN 0743-7463

Full text not available in this repository. Request a copy from the Strathclyde author

Abstract

The mechanism of hen egg white lysozyme (HEWL) adsorption on a negatively charged, hydrophilic surface has been studied using atomistic molecular dynamics (MD) simulation. Sixteen 90 ns trajectories provide adequate data to allow a detailed description of the adsorption process to be formulated. Two distinct adsorption sites have been identified. The main one is located on the N,C-terminal protein face and comprises Arg128 (the crucial one), supplemented by Arg125, Arg5, and Lys1; the minor one is used accidentally and contains only Arg68. Adsorption of this protein is driven by electrostatics, where the orientation of the protein dipole moment defines the direction of protein movement. The diffusion range on the surface depends on protein side-chain penetration through the surface water layers. This is facilitated by the long-range electric field of the charged surface, which can align polar side chains to be perpendicular to the surface. A simulation of adsorption onto a neutral ionic surface shows no such surface water layer penetration. Therefore, protein flexibility is seen to be an important factor, and to adsorb the HEWL has to adjust its structure. Nevertheless, at a flat surface only a slight loss of alpha-helical content is required. The adsorbed HEWL molecule is oriented between side-on and end-on ways, where the angle between the protein long axis (which mostly approximates the dipole moment) and the surface varies between 45 degrees and 90 degrees. Simulations with targeted mutations confirm the picture that emerges from these studies. The active site is located on the opposite face to the main adsorption site; hence, the activity of the immobilized HEWL should not be affected by the surface interactions. Our results provide a detailed insight into the adsorption mechanism and protein mobility at the surface. This knowledge will aid the proper interpretation of experimental results and the design of new experiments and functional systems.