title: Estimation of intrinsically disordered protein shape and time-averaged apparent hydration in native conditions by a combination of hydrodynamic methods.
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.
authors: Unité de Biochimie des Interactions Macromoléculaires, CNRS UMR 3528, Institut Pasteur, Paris, France.
authors: Johanna C
authors: JC
authors: Karst
authors: Ana Cristina
authors: AC
authors: Sotomayor-Pérez
authors: Daniel
authors: D
authors: Ladant
authors: Alexandre
authors: A
authors: Chenal
mesh_terms: D002623:Chemistry Techniques, Analytical / Q000379:methods*; D002850:Chromatography, Gel; D057446:Hydrodynamics; D008027:Light; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification; D012542:Scattering, Radiation; D013053:Spectrophotometry; D013997:Time Factors; D014461:Ultracentrifugation; D014867:Water / Q000737:chemistry
chemical_list: D011506:Proteins; D014867:Water