Estimation of Intrinsically Disordered Protein Shape and Time-Averaged Apparent Hydration in Native Conditions by a Combination of Hydrodynamic Methods

Autor: Daniel Ladant, Alexandre Chenal, Johanna C. Karst, Ana Cristina Sotomayor-Pérez
Přispěvatelé: Biochimie des Interactions Macromoléculaires / Biochemistry of Macromolecular Interactions, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), This work was supported by the Institut Pasteur (Grant PTR374), the Centre National de la Recherche Scientifique (CNRS UMR3528), and the Agence Nationale de la Recherche, programme Jeunes Chercheurs (ANR, grant ANR-09-JCJC-0012)., ANR-09-JCJC-0012,TransloXyaA(2009), Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS)
Rok vydání: 2012
Předmět:
Materials science
Hydrodynamic radius
Intrinsic viscosity
Size-exclusion chromatography
Intrinsically disordered proteins
Protein hydration
Light scattering
MESH: Hydrodynamics
Quantitative Biology::Subcellular Processes
Analytical Ultracentrifugation
03 medical and health sciences
Size exclusion chromatography
MESH: Water
MESH: Proteins
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
MESH: Scattering
Radiation
Shape factor
Protein shape
Static light scattering
Online viscometer
030304 developmental biology
Quantitative Biology::Biomolecules
0303 health sciences
MESH: Spectrophotometry
Time-averaged apparent hydration
Molecular mass
MESH: Time Factors
MESH: Ultracentrifugation
030302 biochemistry & molecular biology
MESH: Chromatography
Gel
MESH: Chemistry Techniques
Analytical
MESH: Light
Chemical physics
Analytical ultracentrifugation
Dynamic light scattering
Zdroj: Methods in Molecular Biology ISBN: 9781461437031
Methods in Molecular Biology
Methods in Molecular Biology, 896, pp.163-77, 2012, ⟨10.1007/978-1-4614-3704-8_10⟩
DOI: 10.1007/978-1-4614-3704-8_10
Popis: International audience; 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.
Databáze: OpenAIRE
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