Course overview

Purified proteins are used in various types of scientific experiments and fields. For example, in structural biology insights into the functional mechanisms can be obtained by elucidating the 3D molecular structure of proteins and protein complexes using technologies such as X-ray crystallography, cryo-EM and NMR. In biochemistry and biophysics, interactions with other proteins, nucleic acids and small molecules can be studied by determining affinities and specificities. Proteins can function as antigens to generate specific antibodies or as reagents in cell biology experiments. Furthermore, recombinant proteins can be used as tool molecules in genomics, chemical biology and microscopy assays. In order for these experiments to produce reliable and biologically relevant results, they must be performed using high-quality proteins that are active, properly folded, in the right oligomeric state and contain correctly inserted co-factors. Ensuring that these parameters are fulfilled requires quality control.

In this course, we want to help the participants to become acquainted with the concept of protein quality control and provide them with an overview of the specific protein requirements for various downstream applications. Different techniques that can be applied for this purpose will be introduced and participants will have the opportunity to get hands-on experience with these technologies.

Modules/resources

Isothermal Titration Calorimetry (ITC) and Dynamic Light Scattering (DLS)
Nano-Differential Scanning Fluorimetry (nano-DSF) and MicroScale Thermophoresis (MST)
Size Exclusion Chromatography coupled to Multi-Angle Light Scattering and Dynamic Light Scattering (SEC-MALS-DLS) and Mass Photometry
Cryo-Electron Microscopy (cryo-EM)

For more information and to register please visit:
https://www.embl.org/about/info/course-and-conference-office/events/PQC22-01/

Please note that the deadline for registration is 6th September 2022.