`In the second edition of Principles I have attempted to maintain the emphasis on basics, while updating the examples to include more recent results from the literature. There is a new chapter providing an overview of extrinisic fluorophores. The discussion of timeresolved measurements has been expanded to two chapters. Quenching has also been expanded in two chapters. Energy transfer and anisotropy have each been expanded to three chapters. There is also a new chapter on fluorescence sensing. To enhance the usefulness of this book as a textbook, most chapters are followed by a set of problems. Sections which describe advanced topics are indicated as such, to allow these sections to be skipped in an introduction course. Glossaries are provided for commonly used acronyms and mathematical symbols. For those wanting additional informtion, the final appendix contains a list of recommended books which expand on various specialized topics.' from the author's Preface

Principles of Fluorescence Spectroscopy

Science & Math

Joseph R. Lakowicz

Biological Sciences

Springer

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.

Topics in Fluorescence Spectroscopy, Vol. 6: Protein Fluorescence

Plenum Pub Corp

The third edition of this established classic text reference builds upon the strengths of its very popular predecessors. Organized as a broadly useful textbook Principles of Fluorescence Spectroscopy, 3rd edition maintains its emphasis on basics, while updating the examples to include recent results from the scientific literature. The third edition includes new chapters on single molecule detection, fluorescence correlation spectroscopy, novel probes and radiative decay engineering. Includes a link to Springer Extras to download files reproducing all book artwork, for easy use in lecture slides. This is an essential volume for students, researchers, and industry professionals in biophysics, biochemistry, biotechnology, bioengineering, biology and medicine.

Springer London, Limited

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Books by Joseph R. Lakowicz

See the best price to sell, buy, or rent books by Joseph R. Lakowicz. BookScouter helps to compare book prices from 25+ online bookstores and 30+ buyback vendors with a single search.

Principles of Fluorescence Spectroscopy

Topics in Fluorescence Spectroscopy, Vol. 6: Protein Fluorescence

Principles of Fluorescence Spectroscopy

Principles of Fluorescence Spectroscopy

Principles of Fluorescence Spectroscopy