Kinetics of Membrane Protein-Detergent Interactions Depend on Protein Electrostatics.

ABSTRACT: Interactions of a membrane protein with a detergent micelle represent a fundamental process with practical implications in structural and chemical biology. Quantitative assessment of the kinetics of protein-detergent complex (PDC) interactions has always been challenged by complicated behavior of both membrane proteins and solubilizing detergents in aqueous phase. Here, we show the kinetic reads of the desorption of maltoside-containing detergents from β-barrel membrane proteins. Using steady-state fluorescence polarization (FP) anisotropy measurements, we recorded real-time, specific signatures of the PDC interactions. The results of these measurements were used to infer the model-dependent rate constants of association and dissociation of the proteomicelles. Remarkably, the kinetics of t

SUBMITTER: Wolfe AJ 

PROVIDER: S-EPMC6193827 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature