ArticleBiopolymers2018
Thermal melt circular dichroism spectroscopic studies for identifying stabilising amphipathic molecules for the voltage-gated sodium channel NavMs.
Article in Biopolymers, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Structural basis of the Meinwald rearrangement catalysed by styrene oxide isomerase.Nature chemistry · 2024Article
- Isothermal chemical denaturation assay for monitoring protein stability and inhibitor interactions.Scientific reports · 2023Article
- Characterization of a New Glucose-Tolerant GH1 β-Glycosidase fromInternational journal of molecular sciences · 2023Article
- Quality Control of Proteins Solubilized from Inclusion Bodies.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Thermostability-based binding assays reveal complex interplay of cation, substrate and lipid binding in the bacterial DASS transporter, VcINDY.The Biochemical journal · 2021Article
- Lipid Membrane Mimetics in Functional and Structural Studies of Integral Membrane Proteins.Membranes · 2021Review
- Tools and methods for circular dichroism spectroscopy of proteins: a tutorial review.Chemical Society reviews · 2021Review
- Sequential purification and characterization of Torpedo californica nAChR-DC supplemented with CHS for high-resolution crystallization studies.Analytical biochemistry · 2020Article
- Solution NMR: A powerful tool for structural and functional studies of membrane proteins in reconstituted environments.The Journal of biological chemistry · 2019Review
- CDtoolX, a downloadable software package for processing and analyses of circular dichroism spectroscopic data.Protein science : a publication of the Protein Society · 2018Article
- Thermal melt circular dichroism spectroscopic studies for identifying stabilising amphipathic molecules for the voltage-gated sodium channel NavMs.Biopolymers · 2018Article
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Authors and funding
3 authors.
Funding
Abstract
Purified integral membrane proteins require amphipathic molecules to maintain their solubility in aqueous solutions. These complexes, in turn, are used in studies to characterise the protein structures by a variety of biophysical and structural techniques, including spectroscopy, crystallography, and cryo-electron microscopy. Typically the amphilphiles used have been detergent molecules, but more recently they have included amphipols, which are polymers of different sizes and compositions designed to create smaller, more well-defined solubilised forms of the membrane proteins. In this study we used circular dichroism spectroscopy to compare the secondary structures and thermal stabilities of the NavMs voltage-gated sodium channel in different amphipols and detergents as a means of identifying amphipathic environments that maximally maintain the protein structure whilst providing a stabilising environment. These types of characterisations also have potential as means of screening for sample types that may be more suitable for crystallisation and/or cryo-electron microscopy structure determinations.
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