A thermodynamic model for interpreting tryptophan excitation-energy-dependent fluorescence spectra provides insight into protein conformational sampling and stability
A. Kwok, I. Camacho, S. Winter, M. Knight, R. Meade, M. van der Kamp, A. Turner, J. O'Hara, J. Mason, A. R. Jones, V. Arcus, C. R. Pudney
The paper develops a thermodynamic model to quantify the relationship between the tryptophan red edge excitation shift effect and protein flexibility, using examples across multiple scales and protein types.
bioRxiv · Sep 9, 2021Biophysics