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Updated: May 29, 2026

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
Published on: April 2, 2015
Sedimentation velocity of intrinsically disordered proteins: what information can we actually obtain?
David J Scott1, Donald J Winzor
1National Centre for Macromolecular Hydrodynamics, School of Biosciences, University of Nottingham, Sutton Bonington, United Kingdom. dj.scott@nottingham.ac.uk
Abstract:
Intrinsically disordered proteins are a challenge to characterise structurally because of their innate flexibility. Hydrodynamic methods such as sedimentation velocity analytical ultracentrifugation have been proposed as methods for their characterisation. By examining in detail this assumption we show that although velocity measurements do yield information on gross conformation, the information is restricted to only the weight averaged sedimentation and diffusion coefficients of the conformational ensemble.
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