Stability and dynamics of domain-swapped bovine-seminal ribonuclease.
The 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.
Chakrabarti
Kalyan S
KS
Molecular Biophysics Unit, Indian Institute of Science, Bangalore-560012, India.
Sanjeev
B S
BS
Vishveshwara
Saraswathi
S
D000818:Animals; D002417:Cattle; D019281:Dimerization; D004722:Endoribonucleases / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism; D004795:Enzyme Stability; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary / Q000502:physiology; D013816:Thermodynamics
D004722:Endoribonucleases; C032523:ribonuclease SPL