Related Experiment Video
Updated: Jul 18, 2026

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides
Published on: June 19, 2012
Stability and dynamics of domain-swapped bovine-seminal ribonuclease
Kalyan S Chakrabarti1, B S Sanjeev, Saraswathi Vishveshwara
1Molecular Biophysics Unit, Indian Institute of Science, Bangalore-560012, India.
Abstract:
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.
Related Concept Videos
RNA Stability
RNA Stability
Ribozymes
Ribozymes can be...
Ribozymes
Ribozymes can be...
Restarting Stalled Replication Forks
Conservation of Protein Domains
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
