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  2. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    The last of the 20 common amino acids to be discovered was threonine in 1935 by William Cumming Rose, who also determined the essential amino acids and established the minimum daily requirements of all amino acids for optimal growth. [15] [16] The unity of the chemical category was recognized by Wurtz in 1865, but he gave no particular name to ...

  3. Aminoacyl-tRNA - Wikipedia

    en.wikipedia.org/wiki/Aminoacyl-tRNA

    Aminoacyl-tRNA (also aa-tRNA or charged tRNA) is tRNA to which its cognate amino acid is chemically bonded (charged). The aa-tRNA, along with particular elongation factors , deliver the amino acid to the ribosome for incorporation into the polypeptide chain that is being produced during translation.

  4. Proteinogenic amino acid - Wikipedia

    en.wikipedia.org/wiki/Proteinogenic_amino_acid

    The strong charge makes these two amino acids prone to be located on the outer hydrophilic surfaces of the proteins; when they are found inside, they are usually paired with a corresponding negatively charged amino acid, e.g., aspartate or glutamate. Leucine: L Leu Leu is essential for humans, and behaves similarly to isoleucine and valine ...

  5. Isoelectric point - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_point

    Amino acids that make up proteins may be positive, negative, neutral, or polar in nature, and together give a protein its overall charge. At a pH below their pI, proteins carry a net positive charge; above their pI they carry a net negative charge.

  6. Arginine - Wikipedia

    en.wikipedia.org/wiki/Arginine

    Arginine is an essential amino acid for birds, as they do not have a urea cycle. [19] For some carnivores, for example cats, dogs [ 20 ] and ferrets, arginine is essential, [ 3 ] because after a meal, their highly efficient protein catabolism produces large quantities of ammonia which need to be processed through the urea cycle, and if not ...

  7. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    [6]: 148 The charge distribution on the substrate and active site must be complementary, which means all positive and negative charges must be cancelled out. Otherwise, there will be a repulsive force pushing them apart. The active site usually contains non-polar amino acids, although sometimes polar amino acids may also occur. [2]

  8. Amino acid activation - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_activation

    Amino acid activation (also known as aminoacylation or tRNA charging) refers to the attachment of an amino acid to its respective transfer RNA (tRNA). The reaction occurs in the cell cytosol and consists of two steps: first, the enzyme aminoacyl tRNA synthetase catalyzes the binding of adenosine triphosphate (ATP) to a corresponding amino acid, forming a reactive aminoacyl adenylate ...

  9. Ion chromatography - Wikipedia

    en.wikipedia.org/wiki/Ion_chromatography

    The amino acids that have negatively charged side chains at pH 7 (pH of water) are glutamate and aspartate. The beads that are negatively charged are called cation exchange resins, as positively charged proteins will be attracted. The amino acids that have positively charged side chains at pH 7 are lysine, histidine and arginine. [48]

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