Abstract
Laser-induced temperature jump relaxation spectroscopy has emerged as a very useful technique to probe the conformational dynamics of biomolecules (protein, DNA, RNA) and the dynamics of the interactions between them. The basic idea behind this approach is that the equilibrium of interconverting chemical species is suddenly perturbed with a temperature jump, forcing the system to establish a new equilibrium point at a higher temperature. The change in the populations of the interconverting species as they evolve in response to the T-jump perturbation can be monitored with a suitable spectroscopic probe attached to the biomolecule. This time-resolved spectroscopy enables us to follow the conformational dynamics of the biomolecules over an enormous time-window from few nanoseconds to several milliseconds.
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Velmurugu, Y. (2017). Methods. In: Dynamics and Mechanism of DNA-Bending Proteins in Binding Site Recognition. Springer Theses. Springer, Cham. https://doi.org/10.1007/978-3-319-45129-9_2
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DOI: https://doi.org/10.1007/978-3-319-45129-9_2
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