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Stability and Dynamics of Domain-Swapped Bovine-Seminal Ribonuclease

Chakrabarti, Kalyan Sundar 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.


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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
Publication: Chemistry and Biodiversity
Publisher: Verlag Helvetica Chimica Acta AG, Zurich
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: 01 Mar 2019 06:53
URI: http://eprints.iisc.ac.in/id/eprint/4048

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