Editing Asparagine (section)

== Structural function in proteins ==
Since the asparagine side-chain can form hydrogen bond interactions with the peptide backbone, asparagine residues are often found near the beginning of [[alpha-helices]] as [[asx turn]]s and [[asx motif]]s, and in similar turn motifs, or as [[amide ring]]s, in [[beta sheet]]s.  Its role can be thought as "capping" the hydrogen bond interactions that would otherwise be satisfied by the polypeptide backbone.{{cn|date=March 2025}}

Asparagine also provides key sites for [[N-linked glycosylation]], modification of the protein chain with the addition of [[carbohydrate]] chains. Typically, a carbohydrate tree can solely be added to an asparagine residue if the latter is flanked on the C side by X-[[serine]] or X-[[threonine]], where X is any amino acid with the exception of [[proline]].<ref>{{cite book |last1=Brooker |first1=Robert |last2=Widmaier |first2=Eric |last3=Graham |first3=Linda |last4=Stiling |first4=Peter |last5=Hasenkampf |first5=Clare |last6=Hunter |first6=Fiona |last7=Bidochka |first7=Michael |last8=Riggs |first8=Daniel | name-list-style = vanc |title=Biology|date=2010|publisher=McGraw-Hill Ryerson|location=United States of America|isbn=978-0-07-074175-1|pages=105–106|edition=Canadian|chapter=Chapter 5: Systems Biology of Cell Organization}}</ref>

Asparagine can be hydroxylated in the HIF1 [[hypoxia-inducible transcription factor]]. This modification inhibits HIF1-mediated gene activation.<ref>{{cite journal | vauthors = Lando D, Peet DJ, Gorman JJ, Whelan DA, Whitelaw ML, Bruick RK | title = FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor | journal = Genes & Development | volume = 16 | issue = 12 | pages = 1466–71 | date = June 2002 | pmid = 12080085 | pmc = 186346 | doi = 10.1101/gad.991402 }}</ref>