Methods in Enzymology Vol.278 Flourescence Spectroscopy

Discussion in 'Methods in Enzymology Book Series' started by gachmosaic, Aug 1, 2016.

  1. gachmosaic

    gachmosaic New Member

    [​IMG]
    The application of luminescence, primarily fluorescence, to the study of protein structure and dynamics has been extensively exploited to facilitate the understanding of complex biological problems. The interest in the application of phosphorescence, however, shows that new and complementary information can be had by careful optical studies of the phosphorescence lifetime. As in the early days of fluorescence spectroscopy in proteins, a complete and rigorous interpretation of the room temperature phosphorescence remains to be developed; nevertheless, it is clear that time-resolved phosphorescence yields new information on proteins in solution, for example, the detection of subtle conformational changes during protein folding, which is outside the sensitivity of earlier techniques. In addition, the great sensitivity of the phosphorescence lifetime to structural changes associated with rigidity and of nearby quenchers suggests that detailed structural information can be obtained when this approach is combined with the power of site-directed mutagenesis or other more biophysical techniques such as energy transfer to attached acceptors.
    • Series: Methods in Enzymology (Book 278)
    • Hardcover: 628 pages
    • Publisher: Academic Press; 1 edition (June 2, 1997)
    • Language: English
    • ISBN-10: 012182179X
    • ISBN-13: 978-0121821791
    • Product Dimensions: 6 x 1.4 x 9 inches
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