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

Sarah H. Osman published experimental data on the structural role of glycans in the SARS-CoV-2 spike protein in 2026. The dataset contains results from hydrogen/deuterium exchange-mass spectrometry analysis of the recombinant 614G HexaPro spike ectodomain before and after enzymatic deglycosylation. It includes measurements of conformational changes, thermal stability, and binding behavior with antibodies and human ACE2.

Use Cases

• Modeling protein conformational dynamics based on hydrogen/deuterium exchange data.
• Analyzing the structural impact of glycosylation site removal on viral fusion machinery.
• Correlating glycan removal with changes in antibody and receptor binding affinity.
• Studying the effect of the D614G mutation on protein rigidity and disorder.

Strengths

• Data is derived from a specific experimental method (hydrogen/deuterium exchange-mass spectrometry).
• Focuses on a well-defined protein construct (recombinant 614G HexaPro spike ectodomain).
• Includes analysis of multiple functional aspects: conformation, stability, and binding.

Limitations

• Dataset is very small at 28.4 KB, indicating limited scope.
• Row count and column-level documentation are absent; field semantics must be inferred after download.
• Description metadata is limited; actual data quality requires manual inspection after download.

Provenance

Source

figshare, author Sarah H. Osman.

Collection Method

Experimental data from PNGase F glycosidase treatment and hydrogen/deuterium exchange-mass spectrometry.

Time Range

Publication date suggests data generation circa 2026.

Freshness

Last updated 2026-04 22 17:11:08; freshness should be verified.

Geography

Geographic origin of the research is unknown.