When.com Web Search

Search results

  1. Results From The WOW.Com Content Network
  2. Peptide bond - Wikipedia

    en.wikipedia.org/wiki/Peptide_bond

    Peptide bond formation via dehydration reaction. When two amino acids form a dipeptide through a peptide bond, [1] it is a type of condensation reaction. [2] In this kind of condensation, two amino acids approach each other, with the non-side chain (C1) carboxylic acid moiety of one coming near the non-side chain (N2) amino moiety of the other.

  3. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    For example, cyanogen bromide cleaves the peptide bond after a methionine. Similar methods may be used to specifically cleave tryptophanyl, aspartyl, cysteinyl, and asparaginyl peptide bonds. Acids such as trifluoroacetic acid and formic acid may be used for cleavage. Like other biomolecules, proteins can also be broken down by high heat alone.

  4. Endopeptidase - Wikipedia

    en.wikipedia.org/wiki/Endopeptidase

    Endopeptidase or endoproteinase are proteolytic peptidases that break peptide bonds of nonterminal amino acids (i.e. within the molecule), in contrast to exopeptidases, which break peptide bonds from end-pieces of terminal amino acids. [1]

  5. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    A peptide bond forms between the amino acid attached to the tRNA in the P site and the amino acid attached to a tRNA in the A site. The formation of a peptide bond requires an input of energy. The two reacting molecules are the alpha amino group of one amino acid and the alpha carboxyl group of the other amino acids.

  6. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    In inteins, the new ester bond is broken by an intramolecular attack by the soon-to-be C-terminal asparagine. Intermolecular transesterification can transfer a whole segment from one polypeptide to another, as is seen in the Hedgehog protein autoprocessing.

  7. Hydrolysis - Wikipedia

    en.wikipedia.org/wiki/Hydrolysis

    As an example, one may consider proteases (enzymes that aid digestion by causing hydrolysis of peptide bonds in proteins). They catalyze the hydrolysis of interior peptide bonds in peptide chains, as opposed to exopeptidases (another class of enzymes, that catalyze the hydrolysis of terminal peptide bonds, liberating one free amino acid at a time).

  8. Proteasome - Wikipedia

    en.wikipedia.org/wiki/Proteasome

    Proteasomes are protein complexes which degrade ubiquitin-tagged proteins by proteolysis, a chemical reaction that breaks peptide bonds. Enzymes that help such reactions are called proteases. Proteasomes are part of a major mechanism by which cells regulate the concentration of particular proteins and degrade misfolded proteins.

  9. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    Proteases, which are themselves proteins, come in several types according to the particular peptide bonds that they cleave as well as their tendency to cleave peptide bonds at the terminus of a protein (exopeptidases) vs peptide bonds at the interior of the protein (endopeptidases). [107] Pepsin is an endopeptidase in the stomach.