title: Deglycosylation induces extensive dynamics changes in α-amylase revealed by hydrogen/deuterium exchange mass spectrometry.
abstract: BACKGROUND
  N-Linked glycosylation plays important roles in modulating protein structure and function. The direct impact of the modification on protein conformation is not yet well understood.
  
  
  METHODS
  Here we probed the dynamic changes following Endo H trimming of high mannose glycans in α-amylase by means of amide hydrogen/deuterium exchange mass spectrometry.
  
  
  RESULTS
  The results revealed that deglycosylation elicited extensive alterations in backbone dynamics, affecting regions both adjacent to and distal from the glycosylation site.
  
  
  CONCLUSIONS
  The overall exchange rate is reduced in the glycosylated state, which indicates rigidity enhancement due to the attached carbohydrates.
authors.affiliation: NovaBioAssays, 52 Dragon Ct, Woburn, MA, 01801, USA.
authors.forename: Chengjie
authors.initials: C
authors.lastname: Ji
authors.forename: Gary
authors.initials: G
authors.lastname: Wei
mesh_terms: D000595:Amino Acid Sequence; D001236:Aspergillus oryzae / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D003903:Deuterium / Q000737:chemistry; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006031:Glycosylation; D006859:Hydrogen / Q000737:chemistry; D013058:Mass Spectrometry / Q000295:instrumentation / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D000516:alpha-Amylases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D005656:Fungal Proteins; D006859:Hydrogen; D003903:Deuterium; D000516:alpha-Amylases