Chakrabarti, Kalyan S and Sanjeev, BS and Vishveshwara, Saraswathi (2004) Stability and Dynamics of Domain-Swapped Bovine-Seminal Ribonuclease. In: Chemistry and Biodiversity, 1 (5). pp. 802-818.
The proteins of the ribonuclease-A (RNase-A) family are monomeric, with the exception of bovineseminal ribonuclease (BS-RNase). BS-RNase is formed by swapping the N-terminal helices across the two monomeric units.Amolecular-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/mainchain (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.
|Item Type:||Journal Article|
|Additional Information:||The copyright belongs to Verlag Helvetica Chimica Acta AG, Zurich.|
|Keywords:||domain swapped;bovine seminal ribonuclease;molecular dynamics;protein water networks|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||22 Nov 2005|
|Last Modified:||19 Sep 2010 04:21|
Actions (login required)