Cargando…
A Thermodynamic Model for Interpreting Tryptophan Excitation-Energy-Dependent Fluorescence Spectra Provides Insight Into Protein Conformational Sampling and Stability
It is now over 30 years since Demchenko and Ladokhin first posited the potential of the tryptophan red edge excitation shift (REES) effect to capture information on protein molecular dynamics. While there have been many key efforts in the intervening years, a biophysical thermodynamic model to quant...
Autores principales: | Kwok, A, Camacho, IS, Winter, S, Knight, M, Meade, RM, Van der Kamp, MW, Turner, A, O’Hara, J, Mason, JM, Jones, AR, Arcus, VL, Pudney, CR |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8681860/ https://www.ncbi.nlm.nih.gov/pubmed/34926581 http://dx.doi.org/10.3389/fmolb.2021.778244 |
Ejemplares similares
-
Red edge excitation shift spectroscopy is highly sensitive to tryptophan composition
por: Warrender, Annmaree K., et al.
Publicado: (2023) -
Systemic tryptophan homeostasis
por: Klaessens, Simon, et al.
Publicado: (2022) -
Allosteric regulation of substrate channeling: Salmonella typhimurium tryptophan synthase
por: Ghosh, Rittik K., et al.
Publicado: (2022) -
Metabolic profiling reveals altered tryptophan metabolism in patients with kawasaki disease
por: Fan, Xue, et al.
Publicado: (2023) -
Different Mechanisms of Catalytic Complex Formation in Two L-Tryptophan Processing Dioxygenases
por: Nienhaus, Karin, et al.
Publicado: (2018)