N O V - ορισμός. Τι είναι το N O V
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Τι (ποιος) είναι N O V - ορισμός

WIKIMEDIA DISAMBIGUATION PAGE
O(N); O(n) (disambiguation)

N-vector model         
SIMPLE SYSTEM OF INTERACTING SPINS ON A CRYSTALLINE LATTICE
O(n) model
In statistical mechanics, the n-vector model or O(n) model is a simple system of interacting spins on a crystalline lattice. It was developed by H.
O-GlcNAc         
  • Chemoenzymatic labeling for the detection of ''O''-GlcNAc. GalT Y289L transfers GalNAz to ''O''-GlcNAc, providing a handle for click chemistry. Various probes can be conjugated via azide-alkyne cycloaddition. Attachment of a PEG5K mass tag allows for visualization of ''O''-GlcNAc stoichiometry.
  • FRET biosensor for ''O''-GlcNAc. Under high ''O''-GlcNAc conditions, GafD will bind the ''O''-GlcNAc group on the CKII peptide substrate, bringing CFP and YFP into proximity for FRET. Various localization sequences can be fused to localize the sensor to various cellular compartments, e.g., nucleus, cytoplasm, and plasma membrane.
  • Structure of IsoTaG probe. Probe consists of a biotin affinity tag (red), a linker (black), an acid-cleavable silane (blue), an isotope recoding motif (green), and an alkyne (purple).
  • Site-directed mutagenesis for manipulating ''O''-GlcNAc. S/T-to-A mutagenesis prevents ''O''-GlcNAc modification at that residue. S/T-to-C mutagenesis allows for generation of the ''S''-GlcNAc modification, a structural analogue of ''O''-GlcNAc that is not readily hydrolyzed by OGA.
  • ''O''-GlcNAcylation of serine and threonine residues is dynamically controlled by OGT and OGA.
  • GalT radiolabeling of cellular proteins with UDP-[<sup>3</sup>H]galactose followed by β-elimination yielded Galβ1-4GlcNAcitol, suggesting that the substrate for GalT was ''O''-GlcNAc. Radiolabeled [<sup>3</sup>H]galactose shown in red.
  • ''Left'': Model of full-length ncOGT in complex with CKII peptide substrate and UDP.<ref name=":5" /> Colors indicate TPR domain (gray), N-terminal region of catalytic domain (light pink), intervening domain (light green), C-terminal region of catalytic domain (light blue), CKII peptide substrate (green), and UDP (cyan). ''Right'': Structure of human OGA D175N dimer in complex with ''O''-GlcNAcylated TAB1 peptide substrate. Monomers shown in blue-white/light yellow with respective peptide substrates in blue/yellow. (PDB: 5VVU)
  • PDB]]: 4GYW)
  • doi-access=free}}</ref>
THE GLYCOSYLATION OF A PROTEIN BY ADDITION OF N-ACETYLGLUCOSAMINE VIA THE O3 ATOM OF PEPTIDYL-THREONINE, FORMING O3-N-ACETYLGLUCOSAMINE-L-THREONINE.
O-linked β-N-acetylglucosamine (O-GlcNAc); O-glcnac; O-linked beta-N-acetylglucosamine; O-Linked β-N-acetylglucosamine; O-GlcNAcylation; O GlcNAc; Oglcnac; O-linked glcnac
O-GlcNAc (short for O-linked GlcNAc or O-linked β-N-acetylglucosamine) is a reversible enzymatic post-translational modification that is found on serine and threonine residues of nucleocytoplasmic proteins. The modification is characterized by a β-glycosidic bond between the hydroxyl group of serine or threonine side chains and N-acetylglucosamine (GlcNAc).
N-hydroxyarylamine O-acetyltransferase         
CLASS OF ENZYMES
EC 2.3.1.118; Acetyl-CoA:N-hydroxyarylamine O-acetyltransferase
In enzymology, a N-hydroxyarylamine O-acetyltransferase () is an enzyme that catalyzes the chemical reaction

Βικιπαίδεια

O(n)

In mathematics, O(n) may refer to:

  • O(n), the orthogonal group
  • Big O notation, indicating the order of growth of some quantity as a function of n or the limiting behavior of a function, e.g. in computational complexity theory
  • The nth tensor power of Serre's twisting sheaf O ( 1 ) {\displaystyle {\mathcal {O}}(1)}