Crystallographic studies under high hydrostatic pressure
Crystallographic studies under high hydrostatic pressure and under moderate gas pressure Protein dynamics and plasticity are intrinsically correlated to functional efficiency.
Moreover, internal cavities present within proteins are crucial for conformational flexibility. Noble gas labelling can be used to map hydrophobic cavities and tunnels and pressure promotes high energy conformers of lower volumes, and is thus an ideal tool to study conformational fluctuations and relationships between local rigidity and overall flexibility.
Combining high hydrostatic pressure crystallography and crystallography under moderate gas pressure allows to determine the most flexible and the most rigid part of a protein in relation with internal cavity modifications. Using these two complementary approaches, we have investigate the determinants of urate oxidase and neuroglobin plasticity. These studies allowed us to probe the allosteric role of an internal cavity close to the active site in urate oxidase and to identify a mechanical nucleus around used by neuroglobin during its conformational transition to achieve coordination.
- Girard et al., Biophys. J. (2010) Structure-funct<wbr>ion perturbation and dissociation of tetrameric urate oxidase by high hydrostatic pressure.
- Colloc'h and Prangé, Febs Letters (2014) Functional relevance of the internal hydrophobic cavity of urate oxidase
- Colloc'h et al., Scient. Rep. (2017) Determinants of neuroglobin plasticity highlighted by joint coarse-grained simulations and high pressure crystallography<wbr>.
- Colloc'h et al., Biophys J. (2017) Mapping hydrophobic tunnels and cavities in neuroglobin with noble gas under pressure.