Computational Studies of Proteins of Biomedical Significance


Computational Studies of Proteins of Biomedical Significance

The overall goal of this research is to understand how the function of proteins of biomedical significance is affected by perturbations either deriving from the environment (such as solvent effects and binding of small molecules) or internal to the protein (such as residue mutation and oxidation). To achieve this goal, these researchers employ a combination of molecular dynamics computer simulations and quantum mechanical calculations to study how the perturbations affect the protein’s structure and dynamics. They are currently working on four projects using MSI.

  • Understand how the allosteric coupling between dystrophin domains is affected by the local solvent environment and by mutations.
  • Identify the mechanism by which allosteric effectors inhibit HIV-1 protease, and test whether the inhibition is additive to the one deriving from orthosteric drug binding.
  • Determine the possible mechanisms by which amino acid oxidation affects protein function by studying the effects of methionine oxidation on the structural dynamics of small peptides and calmodulin.
  • Quantify the effect and identify the mechanism by which amino acid mutations shift the redox potential of azurin

Addressing these problems will help in the development of new targeted therapeutic solutions for the associated health conditions.

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