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  2. Protein pKa calculations - Wikipedia

    en.wikipedia.org/wiki/Protein_pKa_calculations

    Coupled system consisting of three acids. The black curve shows a back-titration event. 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.

  3. Titration curve - Wikipedia

    en.wikipedia.org/wiki/Titration_curve

    A typical titration curve of a diprotic acid, oxalic acid, titrated with a strong base, sodium hydroxide.Both equivalence points are visible. Titrations are often recorded on graphs called titration curves, which generally contain the volume of the titrant as the independent variable and the pH of the solution as the dependent variable (because it changes depending on the composition of the ...

  4. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Composite of titration curves of twenty proteinogenic amino acids grouped by side chain category. For amino acids with uncharged side-chains the zwitterion predominates at pH values between the two pK a values, but coexists in equilibrium with small amounts of net negative and net positive ions.

  5. Bradford protein assay - Wikipedia

    en.wikipedia.org/wiki/Bradford_protein_assay

    This standard curve is then used to determine the concentration of the unknown protein. The following elaborates on how one goes from the standard curve to the concentration of the unknown. First, add a line of best fit, or Linear regression and display the equation on the chart.

  6. Acid–base titration - Wikipedia

    en.wikipedia.org/wiki/Acid–base_titration

    An acid–base titration is a method of quantitative analysis for determining the concentration of Brønsted-Lowry acid or base (titrate) by neutralizing it using a solution of known concentration (titrant). [1] A pH indicator is used to monitor the progress of the acid–base reaction and a titration curve can be constructed. [1]

  7. Sørensen formol titration - Wikipedia

    en.wikipedia.org/wiki/Sørensen_formol_titration

    The Sørensen formol titration(SFT) invented by S. P. L. Sørensen in 1907 [1] is a titration of an amino acid with potassium hydroxide in the presence of formaldehyde. [2] It is used in the determination of protein content in samples. [3] Formol titration equation for amino acids in general

  8. THEMATICS - Wikipedia

    en.wikipedia.org/wiki/THEMATICS

    Specifically it identifies anomalous shapes in the theoretical titration curves of the ionizable amino acids. Biochemically active amino acids tend to have wide buffer ranges and non-sigmoidal titration patterns. While the method predicts biochemically active amino acids successfully, it also provides input features to a machine learning ...

  9. Ramachandran plot - Wikipedia

    en.wikipedia.org/wiki/Ramachandran_plot

    Glycine has only a hydrogen atom for its side chain, with a much smaller van der Waals radius than the CH 3, CH 2, or CH group that starts the side chain of all other amino acids. Hence it is least restricted, and this is apparent in the Ramachandran plot for glycine (see Gly plot in gallery ) for which the allowable area is considerably larger.