Mechanisms of tryptophan fluorescence shifts in proteins.
By James T. Vivian, P. Callis. Biophysical Journal, 2001
1,304 citations recorded by the source corpus.
Subfields: Atomic and Molecular Physics, and Optics, Molecular Biology, Physical and Theoretical Chemistry
View Paper: https://www.semanticscholar.org/paper/af8724b53b74cb0f4290c4d342f470ed2cc05f30
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Citations in the corpus
- Enzymatic preparation and characterization of iron-chelating peptides from anchovy (Engraulis japonicus) muscle protein (2012, background): “Vivian and Callis (2001) proposed that positively charged residues near the benzene end of the tryptophan would produce red-shifted fluorescence in proteins, so results in this study also revealed that more and more ferrous ions were in close proximity to the tryptophan residues during the process o”