Characterizing Virus Structure And Binding

Nano Differential Scanning Calorimetry (Nano DSC) and Isothermal Titration Calorimetry (ITC) are powerful label-free and immobilization free analytic tools for thermodynamic measurements of molecular binding, biomolecular thermostability, and enzyme kinetic reactions.

The self-assembly of viral proteins and nucleic acids to form stable particles, and the mechanisms by which viruses bind to and penetrate host cells, represent two key aspects to understanding the basis of viral infection. The thermal stability of virus coat proteins in solution, compared with the stability of the corresponding highly structured viral protein shell, can be most effectively characterized by Nano DSC, whereas fundamental information about the molecular interactions driving virus/cell binding processes can be obtained by measuring the heat evolved or absorbed during binding using ITC. Here, we review applications of Nano DSC and ITC for studying the stability of virus particles and their binding to cells, as well as for the identification of viruses.