Hydrophobic interactions. Hydrophobic interactions also played a role in stabilizing ligands within H1 ( Figure 9 ) and N1 ( Figure 10 ) binding sites during MD. Due to differences in ligand structure and binding conformation, amino acids with which hydrophobic interactions were formed differed. In H1, amino acids involved in hydrophobic interactions included Pro82, Asp103, Asn104, Cys107, Cys153, and Pro154. More stabilizing interactions including H-bonds and hydrophobic interactions were observed in the N1 binding site (Figure 10 ). For the TCM candidates and Tamiflu, the spatial distribution of H-bonds coupled and hydrophobic interactions limits the free movement of ligands within N1, thus increasing stability of the N1-ligand complex.