The lecture series provides an introduction to proteins starting with the basics of protein structure determination up to structure-function relationship.
- Scattering function of a macromolecule
- Principles of macromolecular crystallography
- Principles of microscopy
- Small angle scattering
- X-ray holography on cells, organelles and complexes
- Electron microscopy on single 2D crystals of bacteriorhodpsin
- Neutron and X-ray diffraction on stacks of 2D crystals of bacteriorhodopsin
- Methods for the creation of 3D crystals of membrane proteins
- Crystal structures of bacteriorhodopsin and sensory rhodopsin/transducer complex
- X-ray diffraction on single crystals of 2D and 3D crystals using Free Electron Lasers
The aim of this lecture is to assess the quality of structural models from the Protein Data Bank (RCSB PDB). The emphasis will be on validation of protein models determined by x-ray crystallographic techniques. We will have a look at possible types of errors and try to find out "what is a good model" and which validation criteria are most commonly used by "producers" and "users". The outline will decide between the overall and the local quality of a model. What information can we get from - for example Free R-value, Ramachandran plot, Real-space fit etc. And: which structural model is more reliable - the one with 1.5 Å data or with 3 Å data?
- X-ray crystallography and protein structure
- Information that can be achieved from high-resolution 3D structure
- Does structure help us understand protein function? (Case studies: Enzymes and non-enzyme proteins)
- Proteins do not function in isolation but are part of complex interaction networks (Case study: Protein complexes)
- Protein structure and misfolding diseases
- Types of motions in proteins
- The function of dynamical properties
- Hierarchy of time scales
- Experimental techniques to study dynamical properties
- Case studies which highlight the functional relevance of protein dynamics
BioSoft