Protein phase behaviour and structure: the effect of buffer isotope composition
When we investigate the properties of proteins with NMR or neutron scattering, we need to partially or completely substitute D2O for H2O as a solvent. In this project we will investigate the structural and macroscopic properties of globular proteins as a function of the buffer D2O-ratio, and compare it with their properties as a function of salt concentration.
During this project the student will learn basic protein preparation and characterisation techniques (UV spectroscopy, UV-Vis; polyacrylamide gel electrophoresis, PAGE; small angle X-ray scattering, SAXS) and analysis tools (molecular modelling of small angle scattering data). A large range of protein concentration will be explored. This will allow the student to learn the basics of protein purification and concentration. At the end of the project, the student will be able to determine the cloud-point of protein solutions, analyse the solution structure of model globular proteins and determine the spinodal temperature and osmotic compressibility. Finally the student will submit a scientific report summarising the main results obtained and the difficulties encountered.