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  2. Peptide - Wikipedia

    en.wikipedia.org/wiki/Peptide

    [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 .

  3. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Intramolecular transesterification, resulting in a branched polypeptide. 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.

  4. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    An assemblage of multiple copies of a particular polypeptide chain can be described as a homomer, multimer or oligomer. Bertolini et al. in 2021 [8] presented evidence that homomer formation may be driven by interaction between nascent polypeptide chains as they are translated from mRNA by nearby adjacent ribosomes.

  5. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    The folding of many proteins begins even during the translation of the polypeptide chain. The amino acids interact with each other to produce a well-defined three-dimensional structure, known as the protein's native state. This structure is determined by the amino-acid sequence or primary structure. [2]

  6. Protein tertiary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_tertiary_structure

    The tertiary structure will have a single polypeptide chain "backbone" with one or more protein secondary structures, the protein domains. Amino acid side chains and the backbone may interact and bond in a number of ways. The interactions and bonds of side chains within a particular protein determine its tertiary structure.

  7. Protein biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Protein_biosynthesis

    Once synthesis of the polypeptide chain is complete, the polypeptide chain folds to adopt a specific structure which enables the protein to carry out its functions. The basic form of protein structure is known as the primary structure, which is simply the polypeptide chain i.e. a sequence of covalently bonded amino acids. The primary structure ...

  8. 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.

  9. Ribbon diagram - Wikipedia

    en.wikipedia.org/wiki/Ribbon_diagram

    Polypeptide direction, NH 2 and COOH termini Small arrows on one or both of the termini, or letters. For β-strands, the direction of the arrow is sufficient. Today, the direction of the polypeptide chain is often indicated by a colour ramp. Disulfide bonds Interlocked SS symbol or a zigzag, like a stylized lightning stroke.