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  2. PEP group translocation - Wikipedia

    en.wikipedia.org/wiki/PEP_group_translocation

    The glucose PTS system in E. coli and B. subtilis. The pathway can be read from right to left, with glucose entering the cell and having a phosphate group transferred to it by EIIB. The mannose PTS in E. coli has the same overall structure as the B. subtilis glucose PTS, i.e. the IIABC domains are fused into one protein.

  3. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Protein anabolism is the process by which proteins are formed from amino acids. It relies on five processes: amino acid synthesis, transcription, translation, post translational modifications, and protein folding. Proteins are made from amino acids. In humans, some amino acids can be synthesized using already existing intermediates. These amino ...

  4. O-linked glycosylation - Wikipedia

    en.wikipedia.org/wiki/O-linked_glycosylation

    Structure of ceramide, galactosylceramide and glucosylceramide. Galactose or glucose sugars can be attached to a hydroxyl group of ceramide lipids in a different form of O-glycosylation, as it does not occur on proteins. [6] This forms glycosphingolipids, which are important for the localisation of receptors in membranes. [8]

  5. Glycosylation - Wikipedia

    en.wikipedia.org/wiki/Glycosylation

    It is a spontaneous reaction and a type of post-translational modification of proteins meaning it alters their structure and biological activity. It is the covalent attachment between the carbonil group of a reducing sugar (mainly glucose and fructose) and the amino acid side chain of the protein. In this process the intervention of an enzyme ...

  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. Oxidative phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Oxidative_phosphorylation

    This ATP synthesis reaction is called the binding change mechanism and involves the active site of a β subunit cycling between three states. [77] In the "open" state, ADP and phosphate enter the active site (shown in brown in the diagram). The protein then closes up around the molecules and binds them loosely – the "loose" state (shown in red).

  8. Protein phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Protein_phosphorylation

    In this way protein dynamics can induce a conformational change in the structure of the protein via long-range allostery with other hydrophobic and hydrophilic residues in the protein. One such example of the regulatory role that phosphorylation plays is the p53 tumor suppressor protein.

  9. Protein isoform - Wikipedia

    en.wikipedia.org/wiki/Protein_isoform

    Protein A, B and C are isoforms encoded from the same gene through alternative splicing. A protein isoform, or "protein variant", [1] is a member of a set of highly similar proteins that originate from a single gene and are the result of genetic differences. [2] While many perform the same or similar biological roles, some isoforms have unique ...