SARS-CoV-2 Spike Protein Glycosylation Effects on Conformational Dynamics

98.3 KB of experimental results on the role of N-glycosylation in the SARS-CoV-2 spike protein's structure and function. The dataset, authored by Sarah H. Osman and last updated in April 2026, contains data from hydrogen/deuterium exchange-mass spectrometry analysis of the recombinant 614G HexaPro spike ectodomain protein following enzymatic deglycosylation.

Use Cases

• Modeling protein conformational changes based on hydrogen/deuterium exchange data.
• Analyzing the impact of glycosylation on antibody and hACE2 binding affinity.
• Studying the structural effects of the D614G mutation and glycan removal on the receptor-binding domain.
• Investigating the role of glycans in viral fusion machinery, as indicated by changes in the heptad repeat 2 region.

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 analysis of multiple structural regions mentioned in the description, such as the 630 loop and fusion peptide proximal region.

Limitations

• Row count is unknown, which may limit suitability assessment.
• Column-level documentation is absent; field semantics must be inferred after download.
• The dataset is very small (98.3 KB), indicating a limited scope of data.

Provenance

Source

figshare

Collection Method

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

Time Range

Experimental study date unknown; dataset last updated April 2026.

Freshness

Last updated 2026-04-22 17:11:06; freshness should be verified.

Geography

Geographic origin of the research is unknown.