| Protein Fluorescence 2000 Edition Contributor(s): Lacowicz, Joseph R. (Editor) |
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ISBN: 0306464519 ISBN-13: 9780306464515 Publisher: Springer OUR PRICE: $161.49 Product Type: Hardcover - Other Formats Published: November 2000 Annotation: This sixth volume in the highly regarded series is an essential addition to libraries serving analytical chemists, spectroscopists, biochemists, and biophysicists. Maintaining the high standards set by its predecessors, Protein Fluorescence presents twelve state-of-the-art chapters by some of the most respected researchers in the field. |
| Additional Information |
| BISAC Categories: - Science | Chemistry - Analytic - Science | Life Sciences - Biochemistry - Medical |
| Dewey: 543.085 |
| LCCN: 91032671 |
| Series: Topics in Fluorescence Spectroscopy |
| Physical Information: 0.86" H x 6.08" W x 9.46" (1.31 lbs) 310 pages |
| Descriptions, Reviews, Etc. |
| Publisher Description: 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. |