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Topics in Fluorescence Spectroscopy

Protein Fluorescence

Editors: Lacowicz, Joseph R. (Ed.)

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About this book

The intrinsic or natural fluorescence of proteins is perhaps the most complex area of biochemical fluorescence. Fortunately the fluorescent amino acids, phenylalanine, tyrosine and tryptophan are relatively rare in proteins. Tr- tophan is the dominant intrinsic fluorophore and is present at about one mole % in protein. As a result most proteins contain several tryptophan residues and even more tyrosine residues. The emission of each residue is affected by several excited state processes including spectral relaxation, proton loss for tyrosine, rotational motions and the presence of nearby quenching groups on the protein. Additionally, the tyrosine and tryptophan residues can interact with each other by resonance energy transfer (RET) decreasing the tyrosine emission. In this sense a protein is similar to a three-particle or mul- particle problem in quantum mechanics where the interaction between particles precludes an exact description of the system. In comparison, it has been easier to interpret the fluorescence data from labeled proteins because the fluorophore density and locations could be controlled so the probes did not interact with each other. From the origins of biochemical fluorescence in the 1950s with Prof- sor G. Weber until the mid-1980s, intrinsic protein fluorescence was more qualitative than quantitative. An early report in 1976 by A. Grindvald and I. Z. Steinberg described protein intensity decays to be multi-exponential. Attempts to resolve these decays into the contributions of individual tryp- phan residues were mostly unsuccessful due to the difficulties in resolving closely spaced lifetimes.

About the authors

Dr. J.R. Lakowicz is Professor of Biochemistry at the University of Maryland School of Medicine and Director of the Center for Fluorescence Spectroscopy. Dr. Lakowicz has published over 400 scientific articles, has edited numerous books, holds 16 issued patents, and is the sole author of the widely used text, Principles of Fluorescence Spectroscopy, also published by Kluwer Academic/Plenum Publishers, now in its Second Edition.

Table of contents (12 chapters)

Table of contents (12 chapters)
  • Intrinsic Fluorescence of Proteins

    Pages 1-15

    Eftink, Maurice R.

  • Spectral Enhancement of Proteins by in vivo Incorporation of Tryptophan Analogues

    Pages 17-42

    Alexander Ross, J. B. (et al.)

  • Room Temperature Tryptophan Phosphorescence as a Probe of Structural and Dynamic Properties of Proteins

    Pages 43-65

    Subramaniam, Vinod (et al.)

  • Azurins and Their Site-Directed Mutants

    Pages 67-81

    Mei, Giampiero (et al.)

  • Barnase: Fluorescence Analysis of A Three Tryptophan Protein

    Pages 83-101

    Engelborghs, Yves (et al.)

Buy this book

eBook $169.00
price for USA in USD (gross)
  • ISBN 978-0-306-47102-5
  • Digitally watermarked, DRM-free
  • Included format: PDF
  • ebooks can be used on all reading devices
  • Immediate eBook download after purchase
Hardcover $219.99
price for USA in USD
  • ISBN 978-0-306-46451-5
  • Free shipping for individuals worldwide
  • Usually dispatched within 3 to 5 business days.
Softcover $219.99
price for USA in USD
  • ISBN 978-1-4757-8194-6
  • Free shipping for individuals worldwide
  • Usually dispatched within 3 to 5 business days.
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Bibliographic Information

Bibliographic Information
Book Title
Protein Fluorescence
Editors
  • Joseph R. Lacowicz
Series Title
Topics in Fluorescence Spectroscopy
Series Volume
6
Copyright
2000
Publisher
Springer US
Copyright Holder
Springer Science+Business Media New York
eBook ISBN
978-0-306-47102-5
DOI
10.1007/b115628
Hardcover ISBN
978-0-306-46451-5
Softcover ISBN
978-1-4757-8194-6
Edition Number
1
Number of Pages
XXI, 310
Topics