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- W2295678468 abstract "Detergents are essential tools for membrane protein manipulation. Micelles formed by detergent molecules have the ability to encapsulate the hydrophobic domains of membrane proteins. The resulting protein-detergent complexes (PDCs) are compatible with the polar environments of aqueous media, making structural and functional analysis feasible. Although a number of novel agents have been developed to overcome the limitations of conventional detergents, most have traditional head groups such as glucoside or maltoside. In this study, we introduce a class of amphiphiles, the PSA/Es with a novel highly branched pentasaccharide hydrophilic group. The PSA/Es conferred markedly increased stability to a diverse range of membrane proteins compared to conventional detergents, indicating a positive role for the new hydrophilic group in maintaining the native protein integrity. In addition, PDCs formed by PSA/Es were smaller and more suitable for electron microscopic analysis than those formed by DDM, indicating that the new agents have significant potential for the structure-function studies of membrane proteins." @default.
- W2295678468 created "2016-06-24" @default.
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- W2295678468 date "2016-03-11" @default.
- W2295678468 modified "2023-10-10" @default.
- W2295678468 title "Highly Branched Pentasaccharide-Bearing Amphiphiles for Membrane Protein Studies" @default.
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- W2295678468 doi "https://doi.org/10.1021/jacs.5b13233" @default.
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