Thorben Poburski

Universität Hamburg
Bundesstraße 43
20146 Hamburg
Room:

 

 

Protein Dynamics under Non-Ambient Conditions
Supervisors: Dr. Alke Meents, Prof. Matthias Rarey

Thorben studied Life Science for his undergraduate studies at the Leibniz University Hannover. For his bachelor thesis, he first got in touch with data science where he was finding a model using machine learning that describes an enzyme-coupled sensor the best. Due to the passion he developed, he decided to do his master's degree in bioinformatics at the Universität Hamburg, where he developed a tool for comparing protein binding sites in his final thesis, which plays a major role in rational drug design.
Protein flexibility plays a central role in enzymatic activities, their regulation, the binding of native ligands and drugs and other biomolecular processes. Therefore, the study of protein dynamics is a prerequisite for understanding these mechanisms. A temperature jump method was developed to obtain time-resolved X-ray crystal structures and thus to analyse proteins in motion. The experimental data obtained can be compared with in silico methods, such as molecular dynamics simulations, to subsequently analyse the effects of various perturbations on protein behaviour, enable predictions of protein dynamics and create generic models of protein flexibility.