1H, 13C, and 15N backbone and side-chain resonance assignments of the Nostoc sp. H-NOX C139A variant in complex with the soluble Guanylyl Cyclase inhibitor Zinc Protoporphyrin IX
Stefanos I Gravalos, Emmanouil N Andreadis, Francesca Cantini, Lucia Banci, Georgios A Spyroulias · 2026
Read 1H, 13C, and 15N backbone and side-chain resonance assignments of the Nostoc sp. H-NOX C139A variant in complex with the soluble Guanylyl Cyclase inhibitor Zinc Protoporphyrin IX by Stefanos I Gravalos, Emmanouil N Andreadis, Francesca Cantini, Lucia Banci, Georgios A Spyroulias (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13506654.txt.
Description
Stefanos Gravalos and colleagues report a 2026 data paper that maps the signals of a bacterial protein using nuclear magnetic resonance. The protein, from a cyanobacterium called Nostoc, senses nitric oxide gas. Its human counterpart helps control an enzyme that relaxes blood vessels. Studying the bacterial version clarifies how that enzyme is switched on and off.
The team worked with a changed form of the protein, bound to a zinc compound that blocks the human enzyme. They recorded signals from the protein's backbone and side chains for three atom types. Such maps let other scientists track how the protein's shape shifts when gases or drugs bind. The paper sets out how the sample was made and what its light-absorption traces look like. It adds a reference dataset for work on new vessel-relaxing drugs.
Catalog record
| CREATOR | Stefanos I Gravalos, Emmanouil N Andreadis, Francesca Cantini, Lucia Banci, Georgios A Spyroulias |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 22 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |