To solve this question, it is necessary to consider the number of protein structures that have been empirically verified and the number of Open reading frames predicted from sequencing data
Explanation:
The most common methodologies used to determine protein 3D structure are nuclear magnetic resonance (NMR) and X-ray crystallography. Although both methods are efficient, the determination of 3D protein structures in physiological conditions is a time and cost-consuming task. Moreover, due to recent advances in bioinformatics and sequencing methodologies, the amount of protein Open Reading Frames predicted from sequencing data (especially obtained from Next Sequencing Generation studies) is many times higher. Indeed, less than 5% of sequenced proteins have an empirically validated 3D structure.
Genes they assort independently if they follow the 9: 3: 3: 1 rule resulting from a dihybrid cross. It shows that the genes are not on the same chromosome and they are not included.
