Molecular dy namics studies on the intera ction of an ionic surf actants with adenosine deaminase

Adeno sine deaminase (E.C.۳.۵.۴.۴) is a monomeric protein (۳۴.۵ kDa), wh ich catalyz es the deamination of adenosine a nd ۲۰-deoxyadenosine nucleosides to their r espective in osine derivative nucleosides and ammonia with a rate e nhancement of ۲ × ۱۰۱۲ relative to the nonenzymatic reaction [۱]. The mechanism of denaturation is due to the binding of charged head groups of the surfactan ts to sites with opposite charge a t the surfa ce of the protein follow ed by unfolding and e xposure of the hydrophobic interior and nume rous hydrophobic bindin g sites [۲,۳ ].The intera ction of ani onic surfacta nts with bi omolecules has been studied earlier [۴]. The ai m of this work was to study the effects of anionic surfactants on the activity of adenosine deam inase by m olecular dynamics.

کلیدواژه ها:

Molecular dynam ics ، anionic surfactants ، adenosine deaminize