Protein biophysics research group

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About us

About us

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Our group has been active since 2021, and our research focuses on the mechanical analysis of biomolecules using laser tweezers and magnetic tweezers and atomic force microscopy. Over the last decades, experiments on single molecules have shown that the behaviour of individual molecules can differ significantly from what is extrapolated from the results obtained when studying molecular populations. This is particularly true for molecular conformational and structural changes in response to mechanical forces at all levels of biological systems. Single-molecule manipulation techniques such as laser tweezers or magnetic tweezers offer the possibility to identify and characterise the different spatial and temporal states present in a given molecular process and to study molecular mechanics. Atomic force microscopy can be used to form topological images of individual molecules, allowing the shape and structure of molecules to be studied at the molecular level.

Research areas

Our main area of research is the nanomechanical study of titin giant protein, which is responsible for the passive elasticity of muscle. We aim to investigate the effect of phosphorylation of titin protein on the structure of the polymer chain. In our experiments, we dephosphorylate titin molecules isolated from muscle tissue with a phosphatase enzyme and investigate the structural changes of titin molecules upon treatment. Our results show that the C-terminal part of the titin chain undergoes dephosphorylation and adopts a compact puffed up structure which is visible as a globular head region in atomic force microscopy images. This information allows us to understand how the degree of phosphorylation of titin induces changes in its structure at the molecular level.