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  2. 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

  3. Miller–Urey experiment - Wikipedia

    en.wikipedia.org/wiki/Miller–Urey_experiment

    Below is a table of amino acids produced and identified in the "classic" 1952 experiment, as analyzed by Miller in 1952 [3] and more recently by Bada and collaborators with modern mass spectrometry, [7] the 2008 re-analysis of vials from the volcanic spark discharge experiment, [7] [55] and the 2010 re-analysis of vials from the H 2 S-rich ...

  4. THEMATICS - Wikipedia

    en.wikipedia.org/wiki/THEMATICS

    Theoretical Microscopic Anomalous Titration Curve Shapes (THEMATICS) is a computational method for predicting the biochemically active amino acids in a protein three-dimensional structure. [1] [2] [3] The method was developed by Mary Jo Ondrechen, James Clifton, and Dagmar Ringe. [4]

  5. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    2-, alpha-, or α-amino acids [21] ... Composite of titration curves of twenty proteinogenic amino acids grouped by side ... In the famous Urey-Miller experiment, ...

  6. Kjeldahl method - Wikipedia

    en.wikipedia.org/wiki/Kjeldahl_method

    If boric acid (or some other weak acid) was used, direct acid–base titration is done with a strong acid of known concentration. HCl or H 2 SO 4 can be used. Indirect back titration is used instead if strong acids were used to make the standard acid solution: strong base of known concentration (like NaOH) is used to neutralize the solution. In ...

  7. Biuret test - Wikipedia

    en.wikipedia.org/wiki/Biuret_test

    The characteristic color of a positive biuret test. In chemistry, the biuret test (IPA: / ˌ b aɪ j ə ˈ r ɛ t /, / ˈ b aɪ j ə ˌ r ɛ t / [1]), also known as Piotrowski's test, is a chemical test used for detecting the presence of at least two peptide bonds in a molecule.

  8. Bradford protein assay - Wikipedia

    en.wikipedia.org/wiki/Bradford_protein_assay

    The entire experiment is done at room temperature. The Bradford protein assay can measure protein quantities as little as 1 to 20 μg. [14] It is an extremely sensitive technique. The dye reagent is a stable ready to use product prepared in phosphoric acid. It can remain at room temperature for up to 2 weeks before it starts to degrade.

  9. Methods to investigate protein–protein interactions - Wikipedia

    en.wikipedia.org/wiki/Methods_to_investigate...

    Isothermal titration calorimetry (ITC), is considered as the most quantitative technique available for measuring the thermodynamic properties of protein–protein interactions and is becoming a necessary tool for protein–protein complex structural studies. This technique relies upon the accurate measurement of heat changes that follow the ...