Calculation of relative binding affinities of fructose 1,6-bisphosphatase mutants with adenosine monophosphate using free energy perturbation method.

Abstract excerpt

The free energy perturbation (FEP) methodology is the most accurate means of estimating relative binding affinities between inhibitors and protein variants. In this article, the importance of hydrophobic and hydrophilic residues to the binding of adenosine monophosphate (AMP) to the fructose 1,6-bisphosphatase (FBPase), a target enzyme for type-II diabetes, was examined by FEP method. Five mutations were made to...

Topics

• Adenosine Monophosphate
• Algorithms
• Binding Sites
• Computer Simulation
• Fructose-Bisphosphatase
• Hydrogen Bonding
• Hydrophobic and Hydrophilic Interactions
• Molecular Conformation
• Mutation
• Thermodynamics