Role of N-Glycosylation in SARS-CoV-2 Spike Glycoprotein Conformational Dynamics

Sarah H. Osman published experimental data on figshare in 2026 investigating the role of glycans in the SARS-CoV-2 spike protein. The 55.0 KB dataset contains results from PNGase F glycosidase treatment and hydrogen/deuterium exchange-mass spectrometry analysis. It shows how enzymatic deglycosylation affected protein conformational dynamics, thermal stability, and binding behavior with antibodies and hACE2.

Use Cases

• Modeling protein conformational changes based on hydrogen/deuterium exchange data mentioned in the description
• Analyzing the relationship between glycosylation and protein stability based on thermal stability results
• Studying antibody and receptor binding affinity alterations following glycan removal
• Investigating the structural impact of the D614G mutation in the context of glycan-mediated rigidification

Strengths

• Data is derived from experimental techniques including PNGase F treatment and hydrogen/deuterium exchange-mass spectrometry.
• The dataset provides specific insights into conformational changes in regions like the 630 loop and heptad repeat 2.
• File size is 55.0 KB, indicating a focused and likely well-structured dataset.

Limitations

• Row count is unknown, which may limit suitability assessment.
• Column-level documentation is absent; field semantics must be inferred after download.
• Description metadata is limited; actual data quality requires manual inspection after download.

Provenance

Source

figshare

Collection Method

Experimental data from PNGase F glycosidase treatment and hydrogen/deuterium exchange-mass spectrometry on the recombinant 614G HexaPro spike ectodomain protein.

Time Range

Experimental timeframe not specified; dataset published in 2026.

Freshness

Last updated 2026-04-22 17:11:05; freshness should be verified.

Geography

Geographic scope of the research institution is unknown.