Stability and dynamics of domain-swapped bovine-seminal ribonuclease

Chakrabarti, Kalyan S. ; Sanjeev, B. S. ; Vishveshwara, Saraswathi (2004) Stability and dynamics of domain-swapped bovine-seminal ribonuclease Chemistry and Biodiversity, 1 (5). pp. 802-818. ISSN 1612-1872

Full text not available from this repository.

Official URL:

Related URL:


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.

Item Type:Article
Source:Copyright of this article belongs to John Wiley and Sons.
ID Code:57097
Deposited On:26 Aug 2011 02:43
Last Modified:26 Aug 2011 02:43

Repository Staff Only: item control page