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  2. Flux balance analysis - Wikipedia

    en.wikipedia.org/wiki/Flux_balance_analysis

    Genes are connected to enzyme-catalyzed reactions by Boolean expressions known as Gene-Protein-Reaction expressions (GPR). Typically a GPR takes the form (Gene A AND Gene B) to indicate that the products of genes A and B are protein sub-units that assemble to form the complete protein and therefore the absence of either would result in deletion ...

  3. Protein biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Protein_biosynthesis

    Protein synthesis is a very similar process for both prokaryotes and eukaryotes but there are some distinct differences. [1] Protein synthesis can be divided broadly into two phases: transcription and translation. During transcription, a section of DNA encoding a protein, known as a gene, is converted into a molecule called messenger RNA (mRNA).

  4. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    Protein before and after folding Results of protein folding. Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits the protein to become biologically functional. [1]

  5. Foldit - Wikipedia

    en.wikipedia.org/wiki/Foldit

    Prof. David Baker, a protein research scientist at the University of Washington, founded the Foldit project.Seth Cooper was the lead game designer. Before starting the project, Baker and his laboratory coworkers relied on another research project named Rosetta [5] to predict the native structures of various proteins using special computer protein structure prediction algorithms.

  6. Post-translational modification - Wikipedia

    en.wikipedia.org/wiki/Post-translational...

    Phosphorylation is highly effective for controlling the enzyme activity and is the most common change after translation. [ 2 ] Many eukaryotic and prokaryotic proteins also have carbohydrate molecules attached to them in a process called glycosylation , which can promote protein folding and improve stability as well as serving regulatory functions.

  7. Protein design - Wikipedia

    en.wikipedia.org/wiki/Protein_design

    Protein design is the rational design of new protein molecules to design novel activity, behavior, or purpose, and to advance basic understanding of protein function. [1] Proteins can be designed from scratch ( de novo design) or by making calculated variants of a known protein structure and its sequence (termed protein redesign ).

  8. TIM barrel - Wikipedia

    en.wikipedia.org/wiki/TIM_barrel

    Lactococcus lactis Dihydroorotate dehydrogenase A (DHODA) ( ) is an example of a TIM barrel possessing β-sheets and extended loops over the C-terminal end of the β-barrel. DHODA catalyzes the oxidation of dihydroorotate to orotate, which is part of the de novo uridine 5'-monophosphate (UMP) synthesis pathway. This oxidation is mediated by ...

  9. Chaperone (protein) - Wikipedia

    en.wikipedia.org/wiki/Chaperone_(protein)

    Synthesis of the long tail fibers depends on the chaperone protein gp57A that is needed for the trimerization of gp34 and gp37, the major structural proteins of the tail fibers. [36] [35] The chaperone protein gp38 is also required for the proper folding of gp37.