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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Thermodynamics of ligand binding to acyl-coenzyme A binding protein studied by titration calorimetry.

Ligand binding to recombinant bovine acyl-CoA binding protein (ACBP) was examined using isothermal microcalorimetry. Microcalorimetric measurements confirm that the binding affinity of acyl-CoA esters for ACBP is strongly dependent on the length of the acyl chain with a clear preference for acyl-CoA esters containing more than eight carbon atoms and that the 3'-phosphate of the ribose accounts for almost half of the binding energy. Binding of acyl-CoA esters, with increasing chain length, to ACBP was clearly enthalpically driven with a slightly unfavorable entropic contribution. Accessible surface areas derived from the measured enthalpies were compared to those calculated from sets of three-dimensional solution structures and showed reasonable correlation, confirming the enthalphically driven binding. Binding of dodecanoyl-CoA to ACBP was studied at various temperatures and was characterized by a weak temperature dependence on delta G zero and a strong enthalpy-entropy compensation. This was a direct consequence of a large heat capacity delta Cp caused by the presence of strong hydrophobic interactions. Furthermore, the binding of dodecanoyl-CoA was studied at various pH values and ionic strengths. The data presented here state that ACBP binds long-chain acyl-CoA esters with very high affinity and suggest that ACBP acts as a housekeeping protein with no pronounced built-in specificity.[1]

References

  1. Thermodynamics of ligand binding to acyl-coenzyme A binding protein studied by titration calorimetry. Faergeman, N.J., Sigurskjold, B.W., Kragelund, B.B., Andersen, K.V., Knudsen, J. Biochemistry (1996) [Pubmed]
 
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