When.com Web Search

Search results

  1. Results From The WOW.Com Content Network
  2. Fluorescence spectroscopy - Wikipedia

    en.wikipedia.org/wiki/Fluorescence_spectroscopy

    Fluorescence spectroscopy (also known as fluorimetry or spectrofluorometry) is a type of electromagnetic spectroscopy that analyzes fluorescence from a sample. It involves using a beam of light, usually ultraviolet light , that excites the electrons in molecules of certain compounds and causes them to emit light; typically, but not necessarily ...

  3. Nano differential scanning fluorimetry - Wikipedia

    en.wikipedia.org/wiki/Nano_differential_scanning...

    Both the fluorescence intensity and the fluorescence maximum strongly depend on the close chemical environment of the tryptophan. [3] Typically, interior tryptophan residues in a more hydrophobic environment exhibit a notable emission red shift from approximately 330 nm to 350 nm upon protein unfolding and exposure to water.

  4. Tryptophan (data page) - Wikipedia

    en.wikipedia.org/wiki/Tryptophan_(data_page)

    The complete data for Tryptophan. General information. Chemical formula: C 11 H 12 N 2 O 2 ... GMD MS Spectrum: Phase behavior. Solid properties.

  5. Tryptophan - Wikipedia

    en.wikipedia.org/wiki/Tryptophan

    Tryptophan is an important intrinsic fluorescent probe (amino acid), which can be used to estimate the nature of the microenvironment around the tryptophan residue. Most of the intrinsic fluorescence emissions of a folded protein are due to excitation of tryptophan residues.

  6. Thermal shift assay - Wikipedia

    en.wikipedia.org/wiki/Thermal_Shift_Assay

    The lifetime of tryptophan fluorescence differs between folded and unfolded protein. Quantification of UV-excited fluorescence lifetimes at various temperature intervals yields a measurement of T m. A prominent advantage of this technique is that no reporter dyes need be added as tryptophan is an intrinsic part of the protein.

  7. Fluorescence in the life sciences - Wikipedia

    en.wikipedia.org/wiki/Fluorescence_in_the_life...

    A simplified Jablonski diagram illustrating the change of energy levels.. The principle behind fluorescence is that the fluorescent moiety contains electrons which can absorb a photon and briefly enter an excited state before either dispersing the energy non-radiatively or emitting it as a photon, but with a lower energy, i.e., at a longer wavelength (wavelength and energy are inversely ...

  8. Aromatic amino acid - Wikipedia

    en.wikipedia.org/wiki/Aromatic_amino_acid

    In plants, the shikimate pathway first leads to the formation of chorismate, which is the precursor of phenylalanine, tyrosine, and tryptophan. These aromatic amino acids are the precursors of many secondary metabolites , all essential to a plant's biological functions, such as the hormones salicylate and auxin .

  9. Intrinsic DNA fluorescence - Wikipedia

    en.wikipedia.org/wiki/Intrinsic_DNA_fluorescence

    The fluorescence spectra of the DNA multimers (composed of more than one nucleobase) does not correspond to the sum of the spectra of their monomeric constituents. Their shape and intensity may be affected by various factors, such as the secondary structure, [ 22 ] the viscosity of the solution, [ 23 ] the duplex size, [ 24 ] or the metal ...