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• W1991717719 abstract "SecA is the dissociatable nucleotide and preprotein binding subunit of the bacterial translocase. The thermodynamics of nucleotide binding to soluble SecA at nucleotide binding site I were determined by isothermal titration calorimetry. Binding of ADP and non-hydrolyzable ATPgammaS is enthalpy-driven (DeltaH(0) of -14.44 and -5.56 kcal/mol, respectively), but is accompanied by opposite entropic contributions (DeltaS(0) of -18.25 and 9.55 cal/mol/K, respectively). ADP binding results in a large change in the heat capacity of SecA (DeltaC(p)=-780 cal/mol/K). It is suggested that ADP binding promotes the interaction between the two thermodynamically discernible domains of SecA which is accompanied by a shielding of hydrophobic surface from solvent." @default.
• W1991717719 created "2016-06-24" @default.
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• W1991717719 date "1999-09-10" @default.
• W1991717719 modified "2023-10-18" @default.
• W1991717719 title "Thermodynamics of nucleotide binding to NBS‐I of the <i>Bacillus subtilis</i> preprotein translocase subunit SecA" @default.
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• W1991717719 doi "https://doi.org/10.1016/s0014-5793(99)01139-4" @default.
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