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  2. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Proteins are often synthesized in an inactive precursor form; typically, an N-terminal or C-terminal segment blocks the active site of the protein, inhibiting its function. The protein is activated by cleaving off the inhibitory peptide. Some proteins even have the power to cleave themselves.

  3. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Absorbed amino acids are typically used to create functional proteins, but may also be used to create energy. [3] They can also be converted into glucose. [4] This glucose can then be converted to triglycerides and stored in fat cells. [5] Proteins can be broken down by enzymes known as peptidases or can break down as a result of denaturation ...

  4. Biomolecular structure - Wikipedia

    en.wikipedia.org/wiki/Biomolecular_structure

    Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function.The structure of these molecules may be considered at any of several length scales ranging from the level of individual atoms to the relationships among entire protein subunits.

  5. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    Each protein has its own unique amino acid sequence that is specified by the nucleotide sequence of the gene encoding this protein. The genetic code is a set of three-nucleotide sets called codons and each three-nucleotide combination designates an amino acid, for example AUG ( adenine – uracil – guanine ) is the code for methionine .

  6. Glycoprotein - Wikipedia

    en.wikipedia.org/wiki/Glycoprotein

    The process of glycosylation (binding a carbohydrate to a protein) is a post-translational modification, meaning it happens after the production of the protein. [3] Glycosylation is a process that roughly half of all human proteins undergo and heavily influences the properties and functions of the protein. [ 3 ]

  7. Biomolecule - Wikipedia

    en.wikipedia.org/wiki/Biomolecule

    When two or more polypeptide chains (either of identical or of different sequence) cluster to form a protein, quaternary structure of protein is formed. Quaternary structure is an attribute of polymeric (same-sequence chains) or heteromeric (different-sequence chains) proteins like hemoglobin , which consists of two "alpha" and two "beta ...

  8. Protein biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Protein_biosynthesis

    Many proteins produced within the cell are secreted outside the cell to function as extracellular proteins. Extracellular proteins are exposed to a wide variety of conditions. To stabilize the 3D protein structure, covalent bonds are formed either within the protein or between the different polypeptide chains in the quaternary structure.

  9. Structural motif - Wikipedia

    en.wikipedia.org/wiki/Structural_motif

    In a chain-like biological molecule, such as a protein or nucleic acid, a structural motif is a common three-dimensional structure that appears in a variety of different, evolutionarily unrelated molecules. [1]