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- W2027761908 endingPage "4585" @default.
- W2027761908 startingPage "4581" @default.
- W2027761908 abstract "Thermodynamic parameters for binding of N-acetylglucosamine (GlcNAc) oligomers to a family 18 chitinase, ChiB of Serratia marcescens, have been determined using isothermal titration calorimetry. Binding studies with oligomers of different lengths showed that binding to subsites -2 and +1 is driven by a favorable enthalpy change, while binding to the two other most important subsites, +2 and +3, is driven by entropy with unfavorable enthalpy. These remarkable unfavorable enthalpy changes are most likely due to favorable enzyme-substrate interactions being offset by unfavorable enthalpic effects of the conformational changes that accompany substrate-binding." @default.
- W2027761908 created "2016-06-24" @default.
- W2027761908 creator A5011374047 @default.
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- W2027761908 date "2010-10-20" @default.
- W2027761908 modified "2023-10-15" @default.
- W2027761908 title "Determination of substrate binding energies in individual subsites of a family 18 chitinase" @default.
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- W2027761908 doi "https://doi.org/10.1016/j.febslet.2010.10.017" @default.
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