Deciphering Functional Mechanisms of Enzymes and Molecular Chaperones by Integrated NMR Spectroscopy

  • 7 October 2021
    4:00 PM
  • University Campus Bohunice (pavilion B11/ seminar room 132)


Prof. Paul Schanda

Groupleader at Insitute of Science and Technology, Austria

"The Schanda group is particularly interested in understanding how biomolecules – primarily proteins – perform their tasks, and how their structural dynamics governs their functions. Their work has several aspects. On the one hand, the group studies a number of puzzling biological questions. For example, how do proteins transport other proteins across the cell, across biological membranes or into membranes? By studying how those proteins – chaperones, receptors, translocases – are structured, how they move and how they interact, they decipher how cells are able to transport large and highly aggregation-prone polypeptides all across the cell and ultimately refold them into their native environment. For example, this work unravels how membrane proteins are getting imported into mitochondria, or how megadalton-large chaperones help other proteins to fold. "

See more information at Prof. Schanda´s research group website.

Hosted by

Lukáš Trantírek

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.

Registration for lunch with the speaker /for Ph.D. students/

The sponsored lunch usually takes place in the Campus River restaurant. Please meet the speaker and other students at 12:45 in the Atrium of CEITEC building E35.

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