Springer Protein Fluorescence - Topics in Fluorescence Spectroscopy

Explore the complex world of biochemical fluorescence with Protein Fluorescence, part of the Topics in Fluorescence Spectroscopy series by Springer. This specialized text focuses on the intrinsic or natural fluorescence found within proteins, a vital area for biochemical research. Because fluorescent amino acids like phenylalanine, tyrosine, and tryptophan are relatively rare in proteins, understanding their specific behaviors is essential. Tryptophan serves as the dominant intrinsic fluorophore, typically present at about one mole percent in protein structures. Most proteins contain several tryptophan residues alongside even more tyrosine residues, each contributing to the overall spectral profile. This book examines how the emission of these residues is influenced by various excited state processes. Readers will gain insights into spectral relaxation, proton loss for tyrosine, rotational motions, and other factors that affect fluorescence. It is a necessary resource for those studying the biochemical properties and molecular dynamics of protein structures.