Skip to Main content Skip to Navigation
Book sections

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.
Document type :
Book sections
Complete list of metadatas

https://hal-pasteur.archives-ouvertes.fr/pasteur-01423306
Contributor : Bénédicte Benedic <>
Submitted on : Thursday, December 29, 2016 - 11:27:12 AM
Last modification on : Monday, January 13, 2020 - 5:08:16 PM

Identifiers

Collections

Citation

Johanna C Karst, Ana Cristina Sotomayor-Pérez, Daniel Ladant, Alexandre Chenal. Estimation of intrinsically disordered protein shape and time-averaged apparent hydration in native conditions by a combination of hydrodynamic methods.. Methods in Molecular Biology, 896, pp.163-77, 2012, ⟨10.1007/978-1-4614-3704-8_10⟩. ⟨pasteur-01423306⟩

Share

Metrics

Record views

101