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Springer Protein Fluorescence: Topics in Fluorescence Spectroscopy Vol. 6

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Description

Protein Fluorescence explores the intrinsic fluorescence of proteins, one of the most complex areas of biochemical fluorescence research. This volume examines the fluorescent amino acids-phenylalanine, tyrosine and tryptophan-which are relatively rare in proteins but crucial for understanding protein behavior. Tryptophan serves as the dominant intrinsic fluorophore, present at approximately one mole percent in protein, meaning most proteins contain several tryptophan residues and even more tyrosine residues. The book details how the emission of each residue is affected by multiple excited state processes including spectral relaxation, proton loss for tyrosine, rotational motions and the presence of nearby quenching molecules. This comprehensive treatment provides essential knowledge for researchers and practitioners working in fluorescence spectroscopy and protein analysis.

Key Features

Protein Fluorescence is the sixth volume in the Topics in Fluorescence Spectroscopy series, offering specialized coverage of intrinsic protein fluorescence phenomena.

The book examines the three primary fluorescent amino acids-phenylalanine, tyrosine and tryptophan-and their roles as natural fluorophores in protein systems.

Detailed analysis of tryptophan as the dominant intrinsic fluorophore, including its prevalence at one mole percent in typical proteins.

Coverage of excited state processes affecting amino acid emission, including spectral relaxation, proton loss mechanisms and rotational dynamics.

Comprehensive treatment of quenching effects and their impact on protein fluorescence measurements and interpretation.

Published by Springer, a leading publisher of scientific and medical literature for healthcare practitioners and research professionals.

Product Specifications

Format
hardcover
Domain
Amazon UK
Release Date
30 November 2000
Listed Since
10 December 2006

Barcode

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