Abstract

This chapter discusses the application of fluorescence techniques in studies of peptide conformations and interactions. Steady-state fluorescence spectroscopy based on continuous excitation of the fluorescent sample has been used for more than two decades to investigate structural and rotational parameters of fluorophore-containing peptides. More recently, improvements in the fluorescence decay measurement by nanosecond fluorometry have made possible the elucidation of conformational and dynamic aspects of polypeptides in greater detail. Fluorescence measurements with peptides require the presence of either natural fluorescent amino acid residues or of extrinsic fluorescent probes covalently attached to appropriate side chains or terminal groups of the peptide under investigation. The chapter highlights the distribution of end-to-end distances and end-to-end diffusion in peptides. In recent years, considerable progress has been made in attempts to solubilize and purify peptide receptors. Because of its high sensitivity, fluorescence spectroscopy will be the method of choice for the characterization of well-defined solubilized receptors.

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