About the lecture

Proteins perform their actions by dynamically sampling many conformations. “Seeing” this protein motion is therefore crucial to understanding their function.

In the first part, I shall answer some intriguing mechanistic questions related to chaperones. How do highly insoluble membrane-proteins travel across an aqueous space before they are inserted into the mitochondrial membranes? How do the chaperones in charge (called “TIM”) carry these highly aggregation-prone polypeptides? How can these complexes bind strongly, yet release efficiently, and do so with some specificity for their “clients”? We show that dynamics is a key requirement to resolve these apparently contradicting requirements.

In the second example, I focus on a half-megadalton-large enzyme complex. I will show how a highly dynamic loop - which is even invisible to crystallography - holds the key to the function of the enzyme. I will also show how NMR is able to probe subtle effects and fundamental biophysical questions, such as the activation of protein motion at very low temperature, and side chain motions.