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  2. Thiophene - Wikipedia

    en.wikipedia.org/wiki/Thiophene

    Thiophene is considered to be aromatic, although theoretical calculations suggest that the degree of aromaticity is less than that of benzene. The "electron pairs" on sulfur are significantly delocalized in the pi electron system. As a consequence of its aromaticity, thiophene does not exhibit the properties seen for conventional sulfides. For ...

  3. Aromatic amino acid - Wikipedia

    en.wikipedia.org/wiki/Aromatic_amino_acid

    Aromatic amino acids, excepting histidine, absorb ultraviolet light above and beyond 250 nm and will fluoresce under these conditions. This characteristic is used in quantitative analysis, notably in determining the concentrations of these amino acids in solution. [1] [2] Most proteins absorb at 280 nm due to the presence of tyrosine and ...

  4. Nuclear magnetic resonance spectroscopy of proteins

    en.wikipedia.org/wiki/Nuclear_magnetic_resonance...

    The continuous chain of protons are the sidechain of the individual amino acids. Thus these two experiments are used to build so called spin systems, that is build a list of resonances of the chemical shift of the peptide proton, the alpha protons and all the protons from each residue ’s sidechain.

  5. Stable isotope composition of amino acids - Wikipedia

    en.wikipedia.org/wiki/Stable_isotope_composition...

    The abundance of 15 N in some amino acids reflects an organism's position in a food web. This is due to the ways organisms metabolize different amino acids when they are consumed. Trophic amino acids (TrAAs) are first deaminated, meaning that the amino group is removed to produce an alpha-keto acid carbon skeleton.

  6. Aromaticity - Wikipedia

    en.wikipedia.org/wiki/Aromaticity

    Two different resonance forms of benzene (top) combine to produce an average structure (bottom). In organic chemistry, aromaticity is a chemical property describing the way in which a conjugated ring of unsaturated bonds, lone pairs, or empty orbitals exhibits a stabilization stronger than would be expected by the stabilization of conjugation alone.

  7. Protein pKa calculations - Wikipedia

    en.wikipedia.org/wiki/Protein_pKa_calculations

    When a protein folds, the titratable amino acids in the protein are transferred from a solution-like environment to an environment determined by the 3-dimensional structure of the protein. For example, in an unfolded protein, an aspartic acid typically is in an environment which exposes the titratable side chain to water.

  8. Tautomer - Wikipedia

    en.wikipedia.org/wiki/Tautomer

    Ring–chain tautomers occur when the movement of the proton is accompanied by a change from an open structure to a ring, such as the open chain and cyclic hemiacetal (typically pyranose or furanose forms) of many sugars. [4]: 102 (See Carbohydrate § Ring-straight chain isomerism.) The tautomeric shift can be described as H−O ⋅ C=O ⇌ O ...

  9. Polythiophene - Wikipedia

    en.wikipedia.org/wiki/Polythiophene

    Deviation from coplanarity may be permanent, resulting from mislinkages during synthesis or especially bulky side chains; or temporary, resulting from changes in the environment or binding. This twist in the backbone reduces the conjugation length, and the separation between energy levels is increased.