Spectroscopy of Biological Molecules: New Directions 1999
DOI: 10.1007/978-94-011-4479-7_8
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Room Temperature Tryptophan Phosphorescence as monitor of internal dynamics of isolated human erythrocyte membranes proteins

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“…One of the sources of phosphorescence in proteins is that arising from the amino acid tryptophan. The signal has been exploited to learn about protein segmental flexibility at room temperature ( Mazhul et al, 1999 ). As a rule, however, the motion of soluble globular proteins in solution is characterized by large amplitudes in the low frequency range, resulting in a marked quenching of their triple state, especially by O 2 .…”
Section: Fluorescence Microscopy To Study the Nanoscale And Mesoscale...mentioning
confidence: 99%
“…One of the sources of phosphorescence in proteins is that arising from the amino acid tryptophan. The signal has been exploited to learn about protein segmental flexibility at room temperature ( Mazhul et al, 1999 ). As a rule, however, the motion of soluble globular proteins in solution is characterized by large amplitudes in the low frequency range, resulting in a marked quenching of their triple state, especially by O 2 .…”
Section: Fluorescence Microscopy To Study the Nanoscale And Mesoscale...mentioning
confidence: 99%