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  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. Peptide synthesis - Wikipedia

    en.wikipedia.org/wiki/Peptide_synthesis

    Peptide synthesis. Coupling of two amino acids in solution. The unprotected amine of one reacts with the unprotected carboxylic acid group of the other to form a peptide bond. In this example, the second reactive group (amine/acid) in each of the starting materials bears a protecting group. In organic chemistry, peptide synthesis is the ...

  4. Protein domain - Wikipedia

    en.wikipedia.org/wiki/Protein_domain

    In molecular biology, a protein domain is a region of a protein 's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins.

  5. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    The other two dihedral angles in the peptide bond determine the local shape assumed by the protein backbone. [ 30 ] : 31 The end with a free amino group is known as the N-terminus or amino terminus, whereas the end of the protein with a free carboxyl group is known as the C-terminus or carboxy terminus (the sequence of the protein is written ...

  6. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    By convention, the primary structure of a protein is reported starting from the amino -terminal (N) end to the carboxyl -terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the laboratory. Protein primary structures can be directly sequenced, or inferred from DNA sequences.

  7. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion. Proteolysis in organisms serves many purposes; for ...

  8. Peptide - Wikipedia

    en.wikipedia.org/wiki/Peptide

    Peptides are short chains of amino acids linked by peptide bonds. [1][2] A polypeptide is a longer, continuous, unbranched peptide chain. [3] Polypeptides that have a molecular mass of 10,000 Da or more are called proteins. [4] Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides.

  9. Protein splicing - Wikipedia

    en.wikipedia.org/wiki/Protein_splicing

    Protein splicing is an intramolecular reaction of a particular protein in which an internal protein segment (called an intein) is removed from a precursor protein with a ligation of C-terminal and N-terminal external proteins (called exteins) on both sides. The splicing junction of the precursor protein is mainly a cysteine or a serine, which ...