Backbone 1H, 15N, and 13C Resonance Assignments and Secondary Structure of a Novel Protein OGL-20PT-358 from Hyperthermophile Thermococcus thioreducens sp. nov.
Year: 2007
Type: article
Abstract: OGL-20P(T)-358 is a novel 66 amino acid residue protein from the hyperthermophile Thermococcus thioreducens sp. nov., strain OGL-20PT, which was collected from the wall of the hydrothermal black smoker in the Rainbow Vent along the mid-Atlantic ridge. This protein, which has no detectable sequence homology with proteins or domains of known function, has a calculated pI of 4.76 and a molecular mass of 8.2 kDa. We report here the backbone 1H, 15N, and 13C resonance assignments of OGL-20PT-358. Assignments are 97.5% (316/324) complete. Chemical shift index was used to determine the secondary structure of the protein, which appears to consist of primarily alpha-helical regions. This work is the foundation for future studies to determine the three-dimensional solution structure of the protein.
Source: Molecules and Cells
Institution: University of Alabama in Huntsville
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $2,500
OpenAlex ID: W2412141301