Abstract
Fluorescence spectroscopy has emerged as one of the most important tools in the study of protein structure and function. Sensitivity of the fluorescence techniques is a major advantage. Although it cannot provide total structure like X-ray crystallography or nuclear magnetic resonance (NMR), the sensitivity of the technique allows one to work at or near the intracellular concentrations of macro-molecules and ligands. This is particularly important for proteins that self-associate at higher concentrations. Although steady-state fluorescence spectra can now be easily obtained and steady-state fluorometers are inexpensive and widely available, they suffer from several disadvantages.
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Roy, S., Bhattacharyya, B. (1995). Fluorescence Spectroscopic Studies of Proteins. In: Biswas, B.B., Roy, S. (eds) Proteins: Structure, Function, and Engineering. Subcellular Biochemistry, vol 24. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1727-0_4
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DOI: https://doi.org/10.1007/978-1-4899-1727-0_4
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