Protein Structural Modeling Explains Rapid Oxidation in Poultry and Fish Myoglobins Compared to Livestock Myoglobins
The bioinformatics approach used in this study suggests that, in addition to physiological reasons, shorter D-helix, larger heme cavity in tilapia and yellowfin tuna, and greater solvent-accessible area in poultry contribute to increased oxidation in myoglobin from poultry and fish compared with myoglobin from livestock species.
Authors
- Ranjith Ramanathan (ORCID: https://orcid.org/0000-0001-7849-4432)
- Surendranath P. Suman (ORCID: https://orcid.org/0000-0001-7523-2146)
- Morgan M. Pfeiffer (ORCID: https://orcid.org/0000-0003-2854-5419)
- Gretchen Gayle Mafi (ORCID: https://orcid.org/0000-0001-6250-8211)
- Greeshma Sreejesh
Institutions
- Oklahoma State University (US)
- University of Kentucky (US)
Publication Details
- Journal
- Proteomes
- Published
- 2025-10-08
- DOI
- https://doi.org/10.3390/proteomes13040050
- Primary Topic
- Hemoglobin structure and function
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Oklahoma State University