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- W2417576905 abstract "G-protein-coupled receptors (GPCRs) are highly dynamic membrane proteins and therefore optimization of detergents for solubilization and purification of GPCRs is an arduous task for extraction from cell membranes. The structural dynamics of GPCRs in detergents will provide key insights into the thermodynamic basis of GPCR stability in detergents. Here we report the structural insights into the stability of adenosine receptor A2AR in various detergent systems with varying tail length. We performed microseconds of atomistic molecular dynamics simulations of the A2AR in the inactive and active-like conformational states, in detergent micelles of DDM (Dodecylmaltoside), DM (Decylmaltoside), NG (Nonylglucoside), and OG (Octylglucoside). The calculated stability of the A2AR in these four detergents correlates well with the experimentally measured stability. Further analysis showed that the A2AR in DDM is less flexible and less dynamic compared to the same receptor in short tail detergents such as NG, and OG micelles. The DDM detergent preserves the helicity of the transmembrane helices in A2AR compared to other short chain detergents. NG and OG systems with shorter alkyl tails lead to unraveling of protein structure and abnormal insertion of detergent into the protein that denatures the functional conformation. We find that longer hydrophobic detergent DDM simulation more closely resembles the bilayer simulations in terms of energetics and interaction dynamics, and the insights gained from this study can be used to optimize detergents prior to experiments for GPCRs solubilization." @default.
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- W2417576905 date "2016-02-01" @default.
- W2417576905 modified "2023-09-28" @default.
- W2417576905 title "Insights into the Stability of GPCRs in Detergent Micelles" @default.
- W2417576905 doi "https://doi.org/10.1016/j.bpj.2015.11.1265" @default.
- W2417576905 hasPublicationYear "2016" @default.
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