How and why internal cavities destabilize proteins

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Proteins are marginally stable as a consequence of the large and opposing contributions from enthalpy and entropy to the folded state. The microscopic contributions to the total system ∆S and ∆H are still highly enigmatic. Here, we use hydrostatic pressure – coupled to NMR spectroscopy detection – to explore the protein energy landscape in residue-specific detail. As the conjugate of pressure is volume, this approach offers a mild and clearly defined perturbation of the system, as opposed to mutagenesis, temperature or denaturants. We could thus directly examine the Van der Waals contribution to stability. Pressure-variation also allowed us to detect several partially unfolded states that consist of cooperative modules, a result that argues for a rather discrete route that connects the folded and unfolded forms of a protein.



Sorbonne Université, room 22-23-401

Mardi 19 Février 2019 12:30
Dr. MULDER Frans
Séminaire Thématique
Unité de rattachement: 
UMR 7203
Equipe de rattachement 7203: 
Equipe 3