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The term intrinsic DNA fluorescence refers to the fluorescence emitted directly by DNA when it absorbs ultraviolet (UV) radiation. It contrasts to that stemming from fluorescent labels that are either simply bound to DNA or covalently attached to it, [1] [2] widely used in biological applications; such labels may be chemically modified, not naturally occurring, nucleobases.
The intrinsic DNA fluorescence is very weak. [1] Alternatively, specific or general proteins, nucleic acids, lipids or small molecules can be "labelled" with an extrinsic fluorophore, a fluorescent dye which can be a small molecule, protein or quantum dot.
Fluorescence in the life sciences is used generally as a non-destructive way of tracking or analysis of biological molecules by means of the fluorescent emission at a specific frequency where there is no background from the excitation light, as relatively few cellular components are naturally fluorescent (called intrinsic or autofluorescence).
The fluorescence of a folded protein is a mixture of the fluorescence from individual aromatic residues. Most of the intrinsic fluorescence emissions of a folded protein are due to excitation of tryptophan residues, with some emissions due to tyrosine and phenylalanine; but disulfide bonds also have appreciable absorption in this wavelength range.
Utilization of the intrinsic fluorescence properties of tryptophan residues in many proteins forms the basis of nanoDSF. The emission wavelengths of tryptophan residues are dependent on the surrounding chemical environment, notably solvation (see solvatochromism ) and therefore differ between folded and unfolded protein, just as with the ...
After binding DNA, the quantum yield of PI is enhanced 20-30 fold, and the excitation/emission maximum of PI is shifted to 535 nm (green) / 617 nm (orange-red). [1] Propidium iodide is used as a DNA stain in flow cytometry to evaluate cell viability or DNA content in cell cycle analysis , [ 2 ] or in microscopy to visualize the nucleus and ...
NanoDSF is a type of differential scanning fluorimetry (DSF) method used to determine conformational protein stability by employing intrinsic tryptophan or tyrosine fluorescence, as opposed to the use of extrinsic fluorogenic dyes that are typically monitored via a qPCR instrument. [1] A nanoDSF assay is also known as a type of Thermal Shift Assay.
Alternatively the intrinsic fluorescence of a sample (i.e., autofluorescence) can be used. [1] In the life sciences fluorescence microscopy is a powerful tool which allows the specific and sensitive staining of a specimen in order to detect the distribution of proteins or other molecules of interest. As a result, there is a diverse range of ...