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- W2087515013 abstract "We characterized the thermodynamics of binding reactions of nucleotides ADP and ATPγS (a nonhydrolyzable analog of ATP) to GroEL in a temperature range of 5°C to 35°C by isothermal titration calorimetry. Analysis with a noncooperative binding model has shown that the bindings of nucleotides are driven enthalpically with binding constants of 7×103 M−1 and 4×104 M−1 for ADP and ATPγS, respectively, at 26°C and that the heat capacity change ΔCp is about 100 cal/mol⋅K for both the nucleotides. The stoichiometries of binding were about 8 and 9 molecules for ADP and ATPγS, respectively, per GroEL tetradecamer at 5°C, and both increased with temperature to reach about 14 (ADP) and 12 (ATPγS) for both nucleotides at 35°C. The absence of initial increase of binding heat as well as Hill coefficient less than 1.2, which were obtained from the fitting to the model curve by assuming positive cooperativity, showed that there was virtually no positive cooperativity in the nucleotide bindings. Incorporating a difference in affinity for the nucleotide (ADP and ATPγS) between the two rings of GroEL into the noncooperative binding model improved the goodness of fitting and the difference in the affinity increased with decreasing temperature." @default.
- W2087515013 created "2016-06-24" @default.
- W2087515013 creator A5034027775 @default.
- W2087515013 creator A5084622218 @default.
- W2087515013 date "1999-05-01" @default.
- W2087515013 modified "2023-10-11" @default.
- W2087515013 title "Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: evidence for noncooperative nucleotide binding" @default.
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- W2087515013 doi "https://doi.org/10.1016/s0167-4838(99)00049-7" @default.
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