<p>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.</p>
Cover Feature: Porous Molecular Capsules as Non‐Polymeric Transducers of Mechanical Forces to Mechanophores (Chem. Eur. J. 7/2020)