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Updated: May 20, 2026

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
Published on: April 28, 2022
Estimation of intrinsically disordered protein shape and time-averaged apparent hydration in native conditions by a
Johanna C Karst1, Ana Cristina Sotomayor-Pérez, Daniel Ladant
1Unité de Biochimie des Interactions Macromoléculaires, CNRS UMR 3528, Institut Pasteur, Paris, France.
Abstract:
Size exclusion chromatography coupled online to a Tetra Detector Array in combination with analytical ultracentrifugation (or with quasi-elastic light scattering) is a useful methodology to characterize hydrodynamic properties of macromolecules, including intrinsically disordered proteins. The time-averaged apparent hydration and the shape factor of proteins can be estimated from the measured parameters (molecular mass, intrinsic viscosity, hydrodynamic radius) by these techniques. Here we describe in detail this methodology and its application to characterize hydrodynamic and conformational changes in proteins.
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