Detergent Desorption of Membrane Proteins Exhibits Two Kinetic Phases.

ABSTRACT: Gradual dissociation of detergent molecules from water-insoluble membrane proteins culminates in protein aggregation. However, the time-dependent trajectory of this process remains ambiguous because the signal-to-noise ratio of most spectroscopic and calorimetric techniques is drastically declined by the presence of protein aggregates in solution. We show that by using steady-state fluorescence polarization (FP) spectroscopy the dissociation of the protein-detergent complex (PDC) can be inspected in real time at detergent concentrations below the critical micelle concentration. This article provides experimental evidence of the coexistence of two distinct phases of the dissociations of detergent monomers from membrane proteins. We first noted a slow detergent predesolvation process, which

SUBMITTER: Wolfe AJ 

PROVIDER: S-EPMC5908730 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature