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• W4296131831 abstract "Abstract Understanding how large, oligomeric protein complexes respond to the binding of small ligands and other proteins is essential for describing the molecular basis of life. This in turn requires a complete characterization of the binding energetics and correlation of thermodynamic data with interacting structures, including effects of small molecules and solvent. However, the size of many protein oligomers, the myriad intermediate ligation states they can populate, and their often complex allosteric regulation typically restrict analysis by traditional methods to low resolution, ensemble averages. Here, we employ variabletemperature electrospray ionization native mass spectrometry to determine the thermodynamics for stepwise binding of up to ATP molecules to the 801 kDa GroEL complex, a tetradecamer chaperonin complex. Binding thermodynamics reveal strong enthalpy-entropy compensation (EEC) and high degrees of cooperativity are observed for formation of GroEL-ATP 7 and GroEL-ATP 14 . These are evidenced by entropically favored ATP binding to the cis ring (formation of GroEL-ATP 1-7 ), with variations in EEC for subsequent binding of ATP to the trans ring (GroEL-ATP 8-14 ), as expected for negative inter-ring cooperativity. Entropy driven ATP binding to the GroEL tetradecamer is consistent with ligand induced conformational changes of the GroEL tetradecamer, though the magnitude of the entropy change suggests that reorganization of GroEL-hydrating water molecules and/or expulsion of water from the GroEL cavity may also play a key role. By determining the thermodynamic signatures for individual ligand binding reactions to the large, nearly MDa GroEL complex, we expand our fundamental view of chaperonin functional chemistry. Moreover, this work and related studies of protein-ligand interactions illustrate unparalleled capabilities of vT-ESI-nMS for thermodynamics studies of protein interactions with ligands, and other molecules, such as proteins and drugs." @default.
• W4296131831 created "2022-09-17" @default.
• W4296131831 creator A5040763385 @default.
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• W4296131831 date "2022-09-15" @default.
• W4296131831 modified "2023-09-30" @default.
• W4296131831 title "Dissecting the Thermodynamics of ATP Binding to GroEL One Nucleotide at a Time" @default.
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• W4296131831 doi "https://doi.org/10.1101/2022.09.13.507831" @default.
• W4296131831 hasPublicationYear "2022" @default.
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