The parathyroid hormone (PTH) is an important protein because of its crucial role in maintaining blood calcium level and in bone metabolism. Molecular dynamics simulations have been used here to investigate the structure of 34 residue protein PTH(1-34) in presence of a denaturant, urea and one osmoprotectant,trimethylamine N-oxide (TMAO). The underlying mechanism of the denaturation process by urea as well protecting action by TMAO has been demonstrated. Although it isevident that urea denatures the protein by direct interaction mechanism, the protecting action by TMAO is a clear consequence of depletion of TMAO from the protein surfaceresulting from relative interaction of TMAO with protein and with water.

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