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- W4361255932 abstract "Peptides form the largest group of ligands that modulate the activity of more than 120 different GPCRs. Among which linear disordered peptide ligands usually undergo significant conformational changes upon binding that is essential for receptor recognition and activation. Conformational selection and induced fit are the extreme mechanisms of coupled folding and binding that can be distinguished by analysis of binding pathways by methods that include NMR. However, the large size of GPCRs in membrane-mimetic environments limits NMR applications. In this review, we highlight advances in the field that can be adopted to address coupled folding and binding of peptide ligands to their cognate receptors." @default.
- W4361255932 created "2023-03-31" @default.
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- W4361255932 date "2023-06-01" @default.
- W4361255932 modified "2023-10-15" @default.
- W4361255932 title "NMR applications to GPCR recognition by peptide ligands" @default.
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- W4361255932 doi "https://doi.org/10.1016/j.coph.2023.102366" @default.
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