AbstractThe proteins of the ribonuclease‐A (RNase‐A) family are monomeric, with the exception of bovine‐seminal ribonuclease (BS‐RNase). BS‐RNase is formed by swapping the N‐terminal helices across the two monomeric units. A molecular‐dynamics (MD) study has been performed on the protein for a simulation time of 5.5 ns to understand the factors responsible for the stability of the dimer. Essential dynamics analysis and motional correlation of the protein atoms yielded the picture of a stabilising, yet flexible, interface. We have investigated the role of intermolecular H‐bonding, protein/water interaction, and protein/water networks in stabilising the dimer. The networks of interchain H‐bonds involving side‐chain/side‐chain or side‐chain/main‐chain (ScHB) interactions between the two chains have also been studied. The ability of protein atoms in retaining particular H2O molecules was investigated as a function of the accessible surface area (ASA), depth, and hydration parameters, as well as their participation in protein/water networks.