STRUCTURAL BIOINFORMATICS STUDY OF THE STRUCTURAL BASIS OF SUBSTRATE SPECIFICITY OF PURINE NUCLEOSIDE PHOSPHORYLASE FROM THERMUS THERMOPHILUS

Abstract

Molecular dynamics simulations were performed for wild-type purine nucleoside phosphorylase in complexes with two substrates (adenosine and guanosine). The MD simulations were also performed for the mutant form of the enzyme with the same substrates. The free energy changes upon the formation of the complexes were evaluated from the molecular dynamics trajectories by the MM-GBSA method.