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The Fluorescence Properties of Aromatic Amino Acids: Their Role in the Understanding of Enzyme Structure and Dynamics

  • Arthur G. Szabo
Part of the Progress in Mathematics book series (NSSA)

Abstract

Fluorescence spectroscopy has been extensively used in studies of enzymes and proteins (1–5). It has been shown to provide insights into important aspects of the interrelationships of enzyme structure, function and dynamics. The reasons for the wide applicability of fluorescence spectroscopy are due to several factors. Fluorescence has a high degree of sensitivity allowing one to work at low concentrations typical of “in vivo” conditions. Since the process depends on the absorption and emission of light energy it is selective, probing only those molecular subunits which have appropriate chromophoric properties. A wide vartiety of information is available including the study of inter and intramolecular interactions; the local environment of the fluorescent chromOphore; conformational heterogeneity; the rates of diffusional processes; the dynamics of the flexibility of the protein segments; and the kinetics of enzymatic processes. These studies have been facilitated by the relative ease of obtaining high quality fluorescence measurements using commercially available instruments.

Keywords

Aromatic Amino Acid Fluorescence Quantum Yield Fluorescence Decay Decay Component Conformational Heterogeneity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1989

Authors and Affiliations

  • Arthur G. Szabo
    • 1
  1. 1.Division of Biological Sciences Protein Biochemistry and SpectroscopyNational Research CouncilOttawaCanada

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