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This non-peptide mechanism, elucidated through cryo-electron microscopy and published in the Proceedings of the National Academy of Sciences in 2020, overturned decades of pharmacological dogma that class B GPCRs could only be meaningfully activated by peptide ligands

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Results The inactive full-length GLP-1R structure The crystallization construct of the full-length human GLP-1R includes all of the thermostabilizing mutations present in the previous inactive GLP-1R TMD structures 13 (Methods, Supplementary Fig

Without the molecular weight, that molar specification cannot be translated into a weighable or pipettable quantity