The ability to utilize detailed knowledge of the structure of proteins and to define their interactions with ligands has enabled many advances in our understanding of biological systems and the rational design of new drugs. The primary technique that yields a detailed description of protein structure is X-ray diffraction analysis. A major challenge to the full exploitation of this powerful technique is that the protein must be first crystallized. A variety of conventional techniques are used to produce protein crystals. Most of the crystallization techniques are based on diffusion of one or more species through either liquid or vapor to bring about supersaturation. In this thesis, we introduced fluid dynamics as a novel strategy to control protein-protein interactions and induce crystallization. Two-dimensional protein crystallization on lipid monolayers at the air/water interface is a well established method. The method entails the specific binding of a protein to a fluid lipid monolayer containing a ligand. The protein studied most extensively by this method is the bacterial protein streptavidin. Streptavidin is a tetrameric protein, where each of the four subunits possess a high binding affinity to biotin.The pH of this buffer was then measured with a pH-meter (Fisher Scientific, Accumet AB15) and found to be 4.34 Ap 0.01. Once the buffer solution was made, it was then filtered to remove any particulates (PES medium, vacuum filter with a poreanbsp;...
|Title||:||Flow Enhanced Protein Crystallization at the Air/water Interface|
|Author||:||Ali Nejatbakhsh Azadani|
|Publisher||:||ProQuest - 2007|