Disordered Proteins: Insights from Polymer Physics
| When |
Mar 17, 2025
from 11:00 to 12:00 |
|---|---|
| Where | Salle des thèses |
| Contact Name | Alexis Poncet |
| Attendees |
Tatiana Morozova |
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Phase separation of disordered proteins resulting in the formation of biocondensates has received significant attention due to its fundamental role in cellular organization and functioning and is sought after in many applications. For instance, the liquid-liquid phase separation of tropoelastin initiates the hierarchical assembly of elastic fibers - key components of the extracellular matrix providing resilience and elasticity to biological tissues. Inspired by the hydrophobic domains (HDs) of tropoelastin, elastin-like polypeptides (ELPs) were derived, exhibiting a similar phase behavior. Employing state-of-the-art atomistic modeling, I will discuss how the structural and dynamical properties of ELPs vary as a function of the concentration in the vicinity of the transition, and which residues are essential for contact formation in multi-chain systems [1]. Next, I will demonstrate the importance of the sequence length as a modulator of conformational properties at a single chain level manifesting in different aggregate states of elastin condensates [2]. Finally, I will show that disordered proteins can behave as entirely different polymers, i.e. coils and globules, in different regions of their free energy landscape using \beta-casein as an example [3].
[1] T.I. Morozova et al, Biomacromolecules, 24 (4), 1912-1923 (2023)
[2] T.I. Morozova et al, J. Phys. Chem. Lett., 15 (43), 10757-10762 (2024)
[3] S. Chakraborty et al, J. Phys. Chem. B, 129, 2359-2369 (2025)