Abstract
Protein structural analysis took a big leap forward with the discovery of aromatic amino acid and protein fluorescence (1–4). The intrinsic fluorescence of proteins is a highly sensitive reporter of conformational change at or near the fluorescent tryptophans (Trp) and tyrosines (Tyr). Phenylalanine also exhibits ultraviolet (UV) fluorescence excitation and emission, with a low quantum yield that becomes insignificant in proteins containing Tyr and Trp. The binding of specific extrinsic fluorescent probes allows the site-specific probing of other microdomains or nonfluorescent side chains. Fluorescence resonance energy transfer measurements serve as a “spectroscopic ruler” to measure intramolecular and intermolecular distances and may also be used to ascertain the magnitude of conformational change on ligand binding, protein folding, and protein-protein interactions ([5]; for basic principles of fluorescence, see ref. 6).
Keywords
- Fluorescence Emission
- Intrinsic Fluorescence
- Fluorescence Emission Maximum
- Allosteric Effector
- Zinc Protoporphyrin
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Hirstch, R.E. (2003). Hemoglobin Fluorescence. In: Nagel, R.L. (eds) Hemoglobin Disorders. Methods in Molecular Biology™, vol 82. Humana Press. https://doi.org/10.1385/1-59259-373-9:133
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