Abstract
In peptides, steady-state fluorescence can be used to measure the intrinsic fluorescence of Trp, Tyr, and Phe residues, as well as associated dyes, which can change upon exposure to different environmental conditions. This technique can be thus used to detect changes in the conformational states of peptides. Time-resolved fluorescence can also be used to study fast motions of peptides and their interactions with fluorescence dyes. Data from several low-resolution spectroscopic techniques, including fluorescence, can be combined to generate an overall picture of peptide structure as a function of environmental conditions.
Mangala R. Liyanage and Kunal Bakshi have contributed equally to this chapter.
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Liyanage, M.R., Bakshi, K., Volkin, D.B., Middaugh, C.R. (2014). Fluorescence Spectroscopy of Peptides. In: Nixon, A. (eds) Therapeutic Peptides. Methods in Molecular Biology, vol 1088. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-673-3_16
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DOI: https://doi.org/10.1007/978-1-62703-673-3_16
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