کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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674727 | 1459573 | 2010 | 5 صفحه PDF | دانلود رایگان |
Inhibition of family 18 chitinases has several interesting applications. To this regard, it is important to understand the dependency of binding energetics with respect to the nature of the ligand as well as the chitinase. We have studied the binding of hexameric N-acetylglucosamine (GlcNAc)6 to both glycon and aglycon subsites in chitinase B (ChiB) of Serratia marcescens and we compare the results with binding of allosamidin to ChiB (glycon subsites only, where products are released) and to chitinase A (ChiA) of S. marcescens (glycon subsites only, where polymeric substrates bind). The ΔGr° values for the three binding processes were identical within experimental errors (−38 kJ/mol) while binding was driven by different factors, being solvation entropy (−T ΔSsolv° = −52.3 ± 1.5 kJ/mol), conformational entropy (−T ΔSconf° −45.2 ± 2.0 kJ/mol) [27], and equal contributions of ΔHr° and −T ΔSsolv° (−23.4 ± 0.9 and −20.4 ± 3.1 kJ/mol) [29], respectively.
Journal: Thermochimica Acta - Volume 511, Issues 1–2, 20 November 2010, Pages 189–193