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http://dx.doi.org/10.1002/advs.202416443 | DOI Listing |
Nat Commun
November 2024
Bio-Organic Chemistry, Departments of Biomedical Engineering and Chemical Engineering & Chemistry, Institute for Complex Molecular Systems, Eindhoven University of Technology, 5600 MB, Eindhoven, The Netherlands.
Eur Phys J E Soft Matter
May 2024
Department of Mathematics, Imperial College London, London, SW7 2AZ, UK.
The aggregation or clustering of proteins and other macromolecules plays an important role in the formation of large-scale molecular assemblies within cell membranes. Examples of such assemblies include lipid rafts, and postsynaptic domains (PSDs) at excitatory and inhibitory synapses in neurons. PSDs are rich in scaffolding proteins that can transiently trap transmembrane neurotransmitter receptors, thus localizing them at specific spatial positions.
View Article and Find Full Text PDFFood Chem
March 2024
Key Laboratory of Environmentally Friendly Chemistry and Applications of Ministry of Education, College of Chemistry, Xiangtan University, Xiangtan 410005, PR China.
The intake of estradiol residue from food will lead to health problems, so the rapid and reliable detection of estradiol residue is essential. Multi-mode assays are inherently self-correcting and self-validating, providing more reliable, interference-resistant, high-fidelity results. Here, we developed a dual-mode method to achieve a rapid, reliable, and sensitive detection of estradiol.
View Article and Find Full Text PDFActa Crystallogr D Struct Biol
March 2023
Laboratory of Biomolecular Research, Paul Scherrer Institute, 5232 Villigen PSI, Switzerland.
Rhodopsin is a G-protein-coupled receptor that detects light and initiates the intracellular signalling cascades that underpin vertebrate vision. Light sensitivity is achieved by covalent linkage to 11-cis retinal, which isomerizes upon photo-absorption. Serial femtosecond crystallography data collected from rhodopsin microcrystals grown in the lipidic cubic phase were used to solve the room-temperature structure of the receptor.
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