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Books > Science & Mathematics > Chemistry > Analytical chemistry > Qualitative analytical chemistry > Chemical spectroscopy, spectrochemistry
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Protein Fluorescence (Hardcover, 2000 ed.)
Loot Price: R4,744
Discovery Miles 47 440
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Protein Fluorescence (Hardcover, 2000 ed.)
Series: Topics in Fluorescence Spectroscopy, 6
Expected to ship within 12 - 17 working days
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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.
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