Detergent Desorption of Membrane Proteins Exhibits Two Kinetic PhasesClick to copy article linkArticle link copied!
- Aaron J. WolfeAaron J. WolfeDepartment of Physics, Syracuse University, 201 Physics Building, Syracuse, New York 13244-1130, United StatesStructural Biology, Biochemistry, and Biophysics Program, Syracuse University, 111 College Place, Syracuse, New York 13244-4100, United StatesMore by Aaron J. Wolfe
- Jack F. GugelJack F. GugelDepartment of Physics, Syracuse University, 201 Physics Building, Syracuse, New York 13244-1130, United StatesMore by Jack F. Gugel
- Min ChenMin ChenDepartment of Chemistry, University of Massachusetts Amherst, 820 LGRT, 710 North Pleasant Street, Amherst, Massachusetts 01003-9336, United StatesMore by Min Chen
- Liviu Movileanu*Liviu Movileanu*Tel: 315-443-8078. Fax: 315-443-9103. E-mail: [email protected]Department of Physics, Syracuse University, 201 Physics Building, Syracuse, New York 13244-1130, United StatesStructural Biology, Biochemistry, and Biophysics Program, Syracuse University, 111 College Place, Syracuse, New York 13244-4100, United StatesDepartment of Biomedical and Chemical Engineering, Syracuse University, 223 Link Hall, Syracuse, New York 13244, United StatesMore by Liviu Movileanu
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 was accompanied by a relatively modest change in the FP anisotropy, suggesting a small number of dissociated detergent monomers from the proteomicelles. This predesolvation phase was followed by a fast detergent desolvation process, which was highlighted by a major alteration in the FP anisotropy. The durations and rates of these phases were dependent on both the detergent concentration and the interfacial PDC interactions. Further development of this approach might lead to the creation of a new semiquantitative method for the assessment of the kinetics of association and dissociation of proteomicelles.
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This article is cited by 5 publications.
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J. Wolfe, Jack F. Gugel, Min Chen, Liviu Movileanu. Kinetics of Membrane Protein–Detergent Interactions Depend on Protein Electrostatics. The Journal of Physical Chemistry B 2018, 122
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- Aaron J. Wolfe, Kyle J. Parella, Liviu Movileanu. High‐Throughput Screening of Protein‐Detergent Complexes Using Fluorescence Polarization Spectroscopy. Current Protocols in Protein Science 2019, 97
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https://doi.org/10.1002/cpps.96
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