ArticleActa crystallographica. Section D, Biological crystallography2015
Memprot: a program to model the detergent corona around a membrane protein based on SEC-SAXS data.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed.
- Unraveling ShuA detergent-induced colloidal behavior in solution: A comprehensive SEC-MALS, SAXS, and SANS study.Protein science : a publication of the Protein Society · 2025Article
- Article
- I-Shaped Dimers of a Plant Chloroplast FInternational journal of molecular sciences · 2023Article
- Mirror proteorhodopsins.Communications chemistry · 2023Article
- Analysis and modeling of SDS and DPC micelle SAXS data for membrane protein solution structure characterization.Data in brief · 2023Article
- Mechanisms of Formation, Structure, and Dynamics of Lipoprotein Discs Stabilized by Amphiphilic Copolymers: A Comprehensive Review.Nanomaterials (Basel, Switzerland) · 2022Review
- Article
- MPBuilder: A PyMOL Plugin for Building and Refinement of Solubilized Membrane Proteins Against Small Angle X-ray Scattering Data.Journal of molecular biology · 2021Article
- Molecular model of a sensor of two-component signaling system.Scientific reports · 2021Article
- Restoring structural parameters of lipid mixtures from small-angle X-ray scattering data.Journal of applied crystallography · 2021Article
- Membrane Protein Structures in Lipid Bilayers; Small-Angle Neutron Scattering With Contrast-Matched Bicontinuous Cubic Phases.Frontiers in chemistry · 2020Article
- A Cholesterol Analog Induces an Oligomeric Reorganization of VDAC.Biophysical journal · 2019Article
- Article
- Contrast-Matching Detergent in Small-Angle Neutron Scattering Experiments for Membrane Protein Structural Analysis and Ab Initio Modeling.Journal of visualized experiments : JoVE · 2018Article
- Human Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids.Biophysical journal · 2018Article
- Solution Structure of an Intramembrane Aspartyl Protease via Small Angle Neutron Scattering.Biophysical journal · 2018Article
- Signaling ammonium across membranes through an ammonium sensor histidine kinase.Nature communications · 2018Article
- Low-Resolution Structure of Detergent-Solubilized Membrane Proteins from Small-Angle Scattering Data.Biophysical journal · 2017Article
- Article
- Isolation and structure-function characterization of a signaling-active rhodopsin-G protein complex.The Journal of biological chemistry · 2017Article
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Abstract
The application of small-angle X-ray scattering (SAXS) to structural investigations of transmembrane proteins in detergent solution has been hampered by two main inherent hurdles. On the one hand, the formation of a detergent corona around the hydrophobic region of the protein strongly modifies the scattering curve of the protein. On the other hand, free micelles of detergent without a precisely known concentration coexist with the protein-detergent complex in solution, therefore adding an uncontrolled signal. To gain robust structural information on such systems from SAXS data, in previous work, advantage was taken of the online combination of size-exclusion chromatography (SEC) and SAXS, and the detergent corona around aquaporin-0, a membrane protein of known structure, could be modelled. A precise geometrical model of the corona, shaped as an elliptical torus, was determined. Here, in order to better understand the correlations between the corona model parameters and to discuss the uniqueness of the model, this work was revisited by analyzing systematic SAXS simulations over a wide range of parameters of the torus.
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