Ontology highlight
ABSTRACT:
SUBMITTER: Kahn PC
PROVIDER: S-EPMC6511832 | biostudies-other | 2019 Jun
REPOSITORIES: biostudies-other
Protein science : a publication of the Protein Society 20190429 6
Capillary dilatometry enables direct measurement of changes in volume, an extensive thermodynamic property. The results provide insight into the changes in hydration that occur upon protein folding, ligand binding, and the interactions of proteins with nucleic acids and other cellular components. Often the entropy change arising from release of hydrating solvent provides the main driving force of a binding reaction. For technical reasons, though, capillary dilatometry has not been as widely used ...[more]