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Updated: May 2, 2026

A Hydrogen-Deuterium Exchange Mass Spectrometry HDX-MS Platform for Investigating Peptide Biosynthetic Enzymes
Published on: May 4, 2020
Deglycosylation induces extensive dynamics changes in α-amylase revealed by hydrogen/deuterium exchange mass
1NovaBioAssays, 52 Dragon Ct, Woburn, MA, 01801, USA.
Rationale:
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.
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