Energetics of the interaction between water and the helical peptide group and its role in determining helix propensities.

@article{Avbelj2000EnergeticsOT,
  title={Energetics of the interaction between water and the helical peptide group and its role in determining helix propensities.},
  author={Franc Avbelj and Peizhi Luo and Robert L. Baldwin},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2000},
  volume={97 20},
  pages={10786-91}
}
The alanine helix provides a model system for studying the energetics of interaction between water and the helical peptide group, a possible major factor in the energetics of protein folding. Helix formation is enthalpy-driven (-1.0 kcal/mol per residue). Experimental transfer data (vapor phase to aqueous) for amides give the enthalpy of interaction with water of the amide group as approximately -11.5 kcal/mol. The enthalpy of the helical peptide hydrogen bond, computed for the gas phase by… CONTINUE READING

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