MD simulation of the polyalanine,17-residue helix (pdb:2I9M) and leucine zipper are carried out based on two set of atomic charges,the standard AMBER charge and the dynamically adjusted polarized protein-specific charge (DPPC) from quantum fragment calculations respectively.The result shows the hydrogen bond energy and the number of water molecules near the hydrogen bond in the first salvation shell have a significantly linear correlation.The correlation coefficients are 0.89,0.78 and 0.81 for polyalanine,2I9M protein,leucine zipper separately under DPPC simulation.And the polyalanine protein have almost same hydrogen bond energies due to they are under the same nonpolar microenvironment.The current study provides strong evidence for the hypothesis that hydrogen bonds are much stronger in a hydrophobic surrounding than in a hydrophilic surrounding.And such significant correlation between hydrogen bond strength and microenvironment polarity suggest the context sensitive of backbone-backbone hydrogen bond strength must be considered in protein folding.However,using the AMBER force filed,there are poor linear relationships and their correlation coefficients are 0.23,0.60,0.49 respectively.