Template talk:Protein primary structure

From WikiProjectMed
Jump to navigation Jump to search
WikiProject iconMolecular Biology Template‑class
WikiProject iconThis template is within the scope of WikiProject Molecular Biology, a collaborative effort to improve the coverage of Molecular Biology on Wikipedia. If you would like to participate, please visit the project page, where you can join the discussion and see a list of open tasks.
TemplateThis template does not require a rating on Wikipedia's content assessment scale.

Untitled

Source Reference Quote:

Encyclopedia of Life Sciences Protein Structure: Unusual Covalent Bonds advanced Nancy L Scott, Pennsylvania State University, University Park, Pennsylvania, USA Juliette T J Lecomte, Pennsylvania State University, University Park, Pennsylvania, USA Copyright © 2005 John Wiley & Sons, Ltd. All rights reserved. DOI: 10.1038/npg.els.0003015 Article Online Posting Date: May 3, 2005


Table 1 The most common covalent modifications of amino acids in proteins

Amino acid Modification or product

  • Arginine: N-methylation, N-glycosylation, glycation, ADP-ribosylation, deimination
  • Asparagine: N-glycosylation, ADP-ribosylation, deamidation, isoaspartic acid formation, isopeptide bond crosslinks
  • Aspartic acid: O-phosphorylation, O-methylation, isoaspartic acid formation
  • Cysteine: S-methylation, S-alkylation, S-phosphorylation, ADP-ribosylation, S-nitrosylation, oxidation (disulfide bond, S-thiolation, sulfenic acid and higher oxidation state), prenylation, palmitoylation
  • Glutamic acid: O-methylation, ADP-ribosylation, pyroglutamate formation, g-carboxylation
  • Glutamine: N-methylation, ADP-ribosylation, deamidation, pyroglutamate formation, isopeptide bond crosslinks
  • Glycine: Myristoylation (N-terminal), isopeptide bond formation
  • Histidine: N-methylation, N-phosphorylation, nucleotidylation, diphthamide formation, collagen crosslinks
  • Lysine: N-acylation, N-acetylation, N-methylation, deamination, imine formation, oxidation to aldehyde, hydroxylation, O-glycosylation, glycation, carbamylation, ubiquitination, sumoylation, collagen and other crosslinks
  • Methionine: oxidation, formylation (N-terminal)
  • Proline: Hydroxylation, O-glycosylation
  • Serine: O-phosphorylation, O-acetylation, O-glycosylation, phosphoglycosylation, selenocysteine formationb
  • Threonine: O-phosphorylation, O-glycosylation, nucleotidylation
  • Tryptophan: C-mannosylation
  • Tyrosine: O-phosphorylation, nucleotidylation, O-glycosylation, halogenation, nitration, sulfation, dityrosine linkage
  • Amino terminus: N-methylation, N-acetylation, N-formylation, glycation, pyroglutamate formation (Gln or Glu), myristoylation (Gly), carbamylation
  • Carboxy terminus: O-methylation, glypiation, amidation, ubiquitination, sumoylation

Dr.saptarshi 13:20, 30 November 2006 (UTC)[reply]

Isodesmosine

Should isodesmosine be included (next to desmosine) as well? --kupirijo (talk) 13:07, 12 November 2020 (UTC)[reply]