Understanding enzymic binding affinity : thermodynamics of binding of benzamidinium chloride inhibitors to trypsin

Understanding enzymic binding affinity is of fundamental scientific importance as well as a prerequisite for structure-based drug design. In this study, the interactions of the serine proteinase trypsin with several artificial, benzamidinium-based inhibitors have been studied in aqueous solutions. In order to evaluate the contributions to binding of a specific part of the inhibitor, the influence of small structural variations in that part was studied. The relatively small variations employed in this study are quite unique compared to other studied in this field, where the often large structural variations lead to difficulties in inferring the precise reason for changes in the thermodynamics of binding. In this study, the complete thermodynamics of binding were obtained using isothermal titration calorimetry over a range of temperatures, which is also an advantage in comparison to studies were only the binding constant at one specific temperature has been assessed. ...

Zie: Summary

	titlepages/contents
	chapter 1
	chapter 2
	chapter 3
	chapter 4
	chapter 5
	chapter 6
	chapter 7
	samenvatting
	summary
	thesis

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