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.
Type de document :
Chapitre d'ouvrage
Methods in Molecular Biology, 896, pp.163-77, 2012, 〈10.1007/978-1-4614-3704-8_10〉
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Contributeur : Bénédicte Benedic <>
Soumis le : jeudi 29 décembre 2016 - 11:27:12
Dernière modification le : jeudi 11 janvier 2018 - 06:25:25

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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〉

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