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Intrinsic Fluorescence of Proteins

  • J. W. Longworth
Part of the NATO Advanced Science Institutes Series book series (NSSA, volume 69)

Abstract

A visible blue phosphorescence was detected from chilled hands which had been exposed to solar radiation and then brought into a darkened room. This was reported, in translation, in the Philosophical Transactions of the Royal Society in 1746.1 Much longer was required before any fluorescence was associated with proteinaceous materials; it was only found just over a century ago in 1852.2 We now know that a part of protein fluorescence is visible but difficult to see.3 Proteins largely fluoresce at 300–400nm in the glass ultraviolet (UV), and instruments are required to detect this radiation. Only after a series of essential devices became available more than 30 years ago, did quantitative spectroscopic studies on protein fluorescence begin. High-pressure xenon plasma arcs provided an intense and stable source of quartz UV radiation (200–300nm) needed to excite protein luminescence. Blazed ruled diffraction gratings could be replicated and so became commercially available. The Fastie mounting permitted construction of monochromators that had large quartz and glass UV radiation throughputs. Sample holders could be made from fused synthetic quartz and so were non-fluorescent. High-gain and UV-sensitive photomultipliers and the necessary stable high-voltage power supplies became commercially available.

Keywords

Aromatic Amino Acid Sperm Whale Folding Pattern Tyrosyl Residue Electronic Energy Transfer 
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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© Springer Science+Business Media New York 1983

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  • J. W. Longworth

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