Ions alter the hydration of peptides, which can lead to changes in peptide conformation.  The hydration of tripeptides with charged side chains are examined, specifically glutamic acid and lysine, since these are two of the most commonly found ionic side chains in proteins.  By calculating the free energy of hydration for each side chain, the relative stability in the different salt solutions can be determined.  This project involves studying the mutation of glutamic acid to alanine in NaCl and KCl.  The mutation of lysine to alanine is studied in salts NaCl, NaClO4, and Na2SO4.  The hydration free energy was calculated using the free energy perturbation simulations. The results from these simulations will be presented.

Free energy perturbation of AEA and AKA to AAA in salt solutions

243rd National Meeting (2012)

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