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  2. Transfer RNA - Wikipedia

    en.wikipedia.org/wiki/Transfer_RNA

    Transfer RNA (abbreviated tRNA and ... On the other end of the tRNA is a covalent attachment to the amino acid corresponding to the anticodon sequence, with each type ...

  3. Amino acid activation - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_activation

    Amino acid activation (also known as aminoacylation or tRNA charging) refers to the attachment of an amino acid to its respective transfer RNA (tRNA). The reaction occurs in the cell cytosol and consists of two steps: first, the enzyme aminoacyl tRNA synthetase catalyzes the binding of adenosine triphosphate (ATP) to a corresponding amino acid, forming a reactive aminoacyl adenylate ...

  4. Aminoacyl tRNA synthetase - Wikipedia

    en.wikipedia.org/wiki/Aminoacyl_tRNA_synthetase

    The synthetase first binds ATP and the corresponding amino acid (or its precursor) to form an aminoacyl-adenylate, releasing inorganic pyrophosphate (PPi).The adenylate-aaRS complex then binds the appropriate tRNA molecule's D arm, and the amino acid is transferred from the aa-AMP to either the 2'- or the 3'-OH of the last tRNA nucleotide (A76) at the 3'-end.

  5. Post-translational modification - Wikipedia

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

    biotinylation: covalent attachment of a biotin moiety using a biotinylation reagent, typically for the purpose of labeling a protein. carbamylation: the addition of Isocyanic acid to a protein's N-terminus or the side-chain of Lys or Cys residues, typically resulting from exposure to urea solutions.

  6. Central dogma of molecular biology - Wikipedia

    en.wikipedia.org/wiki/Central_dogma_of_molecular...

    A second version of the central dogma is popular but incorrect. This is the simplistic DNA → RNA → protein pathway published by James Watson in the first edition of The Molecular Biology of the Gene (1965). Watson's version differs from Crick's because Watson describes a two-step (DNA → RNA and RNA → protein) process as the central ...

  7. Guanylyltransferase - Wikipedia

    en.wikipedia.org/wiki/Guanylyltransferase

    In capping enzymes, a highly conserved lysine residue serves as the catalytic residue that forms a covalent enzyme-GMP complex. [1] The transfer RNA (tRNA) for histidine is unique among eukaryotic tRNAs in requiring the addition of a guanine nucleotide before being aminoacylated by the histidine tRNA synthetase.

  8. Aminoacyl-tRNA - Wikipedia

    en.wikipedia.org/wiki/Aminoacyl-tRNA

    An aminoacyl-tRNA, with the tRNA above the arrow and a generic amino acid below the arrow. Most of the tRNA structure is shown as a simplified, colorful ball-and-stick model; the terminal adenosine and the amino acid are shown as structural formulas.

  9. Post-transcriptional modification - Wikipedia

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

    The pre-mRNA processing at the 3' end of the RNA molecule involves cleavage of its 3' end and then the addition of about 250 adenine residues to form a poly(A) tail.The cleavage and adenylation reactions occur primarily if a polyadenylation signal sequence (5'- AAUAAA-3') is located near the 3' end of the pre-mRNA molecule, which is followed by another sequence, which is usually (5'-CA-3') and ...