About This Webinar

Inclusion of Glycopeptides provides increased sequence coverage

Hydrogen/deuterium exchange mass spectrometry (HDX-MS) can provide precise analysis of a protein’s conformational dynamics across varied states, such as heat-denatured vs. native protein structures, localizing regions that are specifically affected by such conditional changes. Maximizing protein sequence coverage provides high confidence that regions of interest are located by HDX-MS, but one challenge for complete sequence coverage is N-glycosylation sites. The deuteration of peptides post-translationally modified by asparagine-bound glycans (glycopeptides) has not always been identified in previous reports of HDX-MS analyses, causing significant sequence coverage gaps in heavily glycosylated proteins and uncertainty in structural dynamics in many regions throughout a glycoprotein.

This session was recorded in September 2023.

Key Learning Objectives

• Conformational dynamics of the spike glycoprotein from SARS-CoV-2 virus are analyzed and visualized
• The experimental workflow of hydrogen/deuterium exchange mass spectrometry is explained
• Adding glycopeptides from spike to analysis of its conformational dynamics improves detail in visualizations, and fills in coverage gaps reported by previous publications