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Polypeptides Folding: Rules for the Calculation of the Backbone Dihedral Angles φ starting from the Amino Acid Sequence

revised on 19.03.2020, 21:01 and posted on 20.03.2020, 07:44 by Michele Larocca

Protein folding is strictly related to the determination of the backbone dihedral angles and depends on the information contained in the amino acid sequence as well as on the hydrophobic effect. To date, the type of information embedded in the amino acid sequence has not yet been revealed. The present study deals with these problematics and aims to furnish a possible explanation of the information contained in the amino acid sequence, showing and reporting rules to calculate the backbone dihedral angles φ. The study is based on the development of mechanical forces once specific chemical interactions are established among the side chain of the residues in a polypeptide chain. It aims to furnish a theoretical approach to predict backbone dihedral angles which, in the future, may be applied to computational developments focused on the prediction of polypeptide structures.


Email Address of Submitting Author


Planetario Osservatorio Astronomico di Anzi-Basilicata, Anzi (PZ), Italy



ORCID For Submitting Author

Declaration of Conflict of Interest

No Conflict of Interest

Version Notes

New Results