The dependence of the amino acid backbone conformation on the translated synonymous codon is not statistically significant

成果类型:
Article
署名作者:
Gonzalez-Delgado, Javier; Mier, Pablo; Bernado, Pau; Neuvial, Pierre; Cortes, Juan
署名单位:
Universite de Rennes; Ecole Nationale de la Statistique et de l'Analyse de l'Information (ENSAI); Centre National de la Recherche Scientifique (CNRS); Consejo Superior de Investigaciones Cientificas (CSIC); Universidad Pablo de Olavide; CSIC - Andalusian Center for Developmental Biology (CABD); Institut National de la Sante et de la Recherche Medicale (Inserm); Universite de Montpellier; Centre National de la Recherche Scientifique (CNRS); Universite de Toulouse; Universite Toulouse III - Paul Sabatier; Centre National de la Recherche Scientifique (CNRS); Universite de Toulouse; Centre National de la Recherche Scientifique (CNRS)
刊物名称:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
ISSN/ISSBN:
0027-9639
DOI:
10.1073/pnas.2503264122
发表日期:
2025-06-17
关键词:
secondary structure protein usage
摘要:
The correlation between synonymous codon usage and secondary structure in translated proteins has been widely demonstrated. This usage plays a capital role in tuning translational rates and protein folding kinetics, indirectly influencing multiple Nat. Commun. 13, 2815 (2022).] suggests that the translated synonymous codon influences the (tp, ) dihedral angles within secondary structure elements. If true, this conclusion would have strong consequences in several scientific fields, including structural biology and protein design, where results would depend on DNA sequence rather than protein sequence. Here, we show that the original statistical methodology used in the referred study was formally incorrect. Furthermore, when using a correct approach, we demonstrate that the influence of the codon on the distribution of the dihedral angles is not statistically significant for any type of secondary structure.