title: Sedimentation velocity analytical ultracentrifugation for intrinsically disordered proteins.
abstract: The size of intrinsically disordered proteins (IDPs) is large compared to their molecular mass and the resulting mass-to-size ratio is unusual. The sedimentation coefficient, which can be obtained from sedimentation velocity (SV) analytical ultracentrifugation (AUC), is directly related to this ratio and can be easily interpreted in terms of frictional ratio. This chapter is a step-by-step protocol for setting up, executing and analyzing SV experiments in the context of the characterization of IDPs, based on a real case study of the partially folded C-terminal domain of Sendai virus nucleoprotein.
authors: Institut de Biologie Structurale, CEA-CNRS-Université, Grenoble, France.
authors: Andrés G
authors: AG
authors: Salvay
authors: Guillaume
authors: G
authors: Communie
authors: Christine
authors: C
authors: Ebel
mesh_terms: D009698:Nucleoproteins / Q000737:chemistry / Q000302:isolation & purification; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D014461:Ultracentrifugation / Q000379:methods*; D014764:Viral Proteins / Q000737:chemistry / Q000302:isolation & purification
chemical_list: D009698:Nucleoproteins; D011506:Proteins; D014764:Viral Proteins