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  2. Amide - Wikipedia

    en.wikipedia.org/wiki/Amide

    Amides are stable to water, and are roughly 100 times more stable towards hydrolysis than esters. [citation needed] Amides can, however, be hydrolyzed to carboxylic acids in the presence of acid or base. The stability of amide bonds has biological implications, since the amino acids that make up proteins are linked with amide

  3. Peptide synthesis - Wikipedia

    en.wikipedia.org/wiki/Peptide_synthesis

    The established method for the production of synthetic peptides in the lab is known as solid phase peptide synthesis (SPPS). [2] Pioneered by Robert Bruce Merrifield , [ 4 ] [ 5 ] SPPS allows the rapid assembly of a peptide chain through successive reactions of amino acid derivatives on a macroscopically insoluble solvent-swollen beaded resin ...

  4. Amide (functional group) - Wikipedia

    en.wikipedia.org/wiki/Amide_(functional_group)

    Structures of three kinds of amides: an organic amide (carboxamide), a sulfonamide, and a phosphoramide. In chemistry, the term amide (/ ˈ æ m aɪ d / or / ˈ æ m ɪ d / or / ˈ eɪ m aɪ d /) [1] [2] [3] is a compound with the functional group R n E(=O) x NR 2, where x is not zero, E is some element, and each R represents an organic group or hydrogen. [4]

  5. Amide ring - Wikipedia

    en.wikipedia.org/wiki/Amide_ring

    An 11-atom amide ring, involving a glutamine residue, occurs at the interior of the light chain variable domains of some Immunoglobulin G antibodies and assists in linking the two beta-sheets. An amide ring is employed in the specificity of the adaptor protein GRB2 for a particular asparagine within proteins it binds.

  6. Deamidation - Wikipedia

    en.wikipedia.org/wiki/Deamidation

    In a protein or peptide, these reactions are important because they may alter its structure, stability or function and may lead to protein degradation. The net chemical change is the addition of a water group and removal of an ammonia group, which corresponds to a +1 (0.98402) Da mass increase.

  7. Chemical chaperone - Wikipedia

    en.wikipedia.org/wiki/Chemical_chaperone

    Chemical chaperones are a broad and diverse group of molecules, and they can influence protein stability and polypeptide organization through a variety of mechanisms. Chemical chaperones are used for a range of applications, from production of recombinant proteins to treatment of protein misfolding in vivo.

  8. Amidase - Wikipedia

    en.wikipedia.org/wiki/Amidase

    In enzymology, an amidase (EC 3.5.1.4, acylamidase, acylase (misleading), amidohydrolase (ambiguous), deaminase (ambiguous), fatty acylamidase, N-acetylaminohydrolase (ambiguous)) is an enzyme that catalyzes the hydrolysis of an amide. In this way, the two substrates of this enzyme are an amide and H 2 O, whereas its two products are ...

  9. Protein production - Wikipedia

    en.wikipedia.org/wiki/Protein_production

    Protein production is the biotechnological process of generating a specific protein. It is typically achieved by the manipulation of gene expression in an organism such that it expresses large amounts of a recombinant gene .