SARS-CoV-2 Spike Protein Glycosylation Effects on Conformation and Stability

Sarah H. Osman's dataset contains results from a study on the role of N-glycosylation in the SARS-CoV-2 spike glycoprotein. The data, last updated in April 2026, includes measurements from hydrogen/deuterium exchange-mass spectrometry experiments on the recombinant 614G HexaPro spike ectodomain protein before and after enzymatic deglycosylation. It provides insights into conformational changes, thermal stability, and binding behavior related to glycan removal.

Use Cases

• Analyze protein conformational dynamics based on hydrogen/deuterium exchange data mentioned in the description
• Investigate the relationship between glycosylation and thermal stability of the spike protein
• Study the impact of glycan removal on antibody and hACE2 receptor binding behavior
• Model the structural role of glycans in specific regions like the 630 loop and heptad repeat 2

Strengths

• Data is derived from a specific experimental method: hydrogen/deuterium exchange-mass spectrometry
• Focuses on a well-defined protein construct: the recombinant 614G HexaPro spike ectodomain
• Includes comparative analysis before and after PNGase F glycosidase treatment

Limitations

• Row count is unknown, which may limit suitability assessment
• Column-level documentation is absent; field semantics must be inferred after download
• Dataset is very small at 12.4 KB, indicating limited scope

Provenance

Source

figshare

Collection Method

Experimental data from PNGase F treatment and hydrogen/deuterium exchange-mass spectrometry on recombinant protein

Time Range

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Freshness

Last updated 2026-04-22 17:11:03; freshness should be verified

Geography

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