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  2. Ramachandran plot - Wikipedia

    en.wikipedia.org/wiki/Ramachandran_plot

    In biochemistry, a Ramachandran plot (also known as a Rama plot, a Ramachandran diagram or a [φ,ψ] plot), originally developed in 1963 by G. N. Ramachandran, C. Ramakrishnan, and V. Sasisekharan, [1] is a way to visualize energetically allowed regions for backbone dihedral angles ( also called as torsional angles , phi and psi angles ) ψ ...

  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. THEMATICS - Wikipedia

    en.wikipedia.org/wiki/THEMATICS

    It is based on computed electrostatic and chemical properties of the individual amino acids in a protein structure. 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.

  5. 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.

  6. Salt bridge (protein and supramolecular) - Wikipedia

    en.wikipedia.org/wiki/Salt_bridge_(protein_and...

    Titration curve between the wild-type (blue) and the mutant (red) The second method utilizes nuclear magnetic resonance spectroscopy to calculate the free energy of the salt bridge. A titration is performed, while recording the chemical shift corresponding to the protons of the carbon adjacent to the carboxylate or ammonium group.

  7. 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.

  8. Titration - Wikipedia

    en.wikipedia.org/wiki/Titration

    A titration curve is a curve in graph the x-coordinate of which represents the volume of titrant added since the beginning of the titration, and the y-coordinate of which represents the concentration of the analyte at the corresponding stage of the titration (in an acid–base titration, the y-coordinate usually represents the pH of the solution).

  9. 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]