Tyrosine Fluorescence and Phosphorescence from Proteins and Polypeptides

Tyrosine Fluorescence and Phosphorescence from Proteins and Polypeptides
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蛋白质和多肽的酪氨酸荧光和磷光

DOI:
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发表时间:
2002
期刊:
影响因子:
--
通讯作者:
H. Wyssbrod
H. Wyssbrod
中科院分区:
--
文献类型:
--
作者:
J. Ross;W. Laws;K. Rousslang;H. Wyssbrod

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The fluorescence and phosphorescence of proteins and polypeptides is the sum of the contributions from the three aromatic amino acids tryptophan, tyrosine, and phenylalanine. The work on protein and polypeptide luminescence prior to 1971 has been reviewed in detail by Longworth. Another fine account of the early work, emphasizing tryptophan and tyrosine, is the monograph by Konev. An excellent review on tyrosine fluorescence in proteins and model peptides, for the period up to 1975, is given by Cowgill. In 1984, Creed reviewed the photophysics and photochemistry of tyrosine and its simple derivatives, including a thorough coverage of steady-state fluorescence and a brief discussion of triplet-state properties, but did not include any work on proteins or polypeptides. The first quantitative studies of the excited-state properties of the three aromatic amino acids were carried out in the 1950s. The low-temperature phosphorescence of the aromatic amino acids was initially observed by Debye and Edwards in 1952, and phosphorescence emission spectra were reported by Steele and Szent-Gyorgyi in 1957. In 1953, Weber postulated that the fluorescence of the aromatic amino acids should occur in the near-ultraviolet region of the electromagnetic spectrum. In 1956, independently and almost simultaneously, Duggan and Udenfriend and Shore and Pardee reported the results of their investigations of protein fluorescence. At the same time,
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影响因子: --
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DOI: --
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