Thermodynamics of mechanopeptide sidechains

Biological systems are often exposed to mechanical perturbations, which may modulate many biochemical processes. Ligand binding involves a wide range of structural changes in the receptor protein, from hinge movement entire domains minor sidechain rearrangements pocket residues. Hydrophobic ligand protein alters system’s vibrational free energy, allowing different conformational states allosteric proteins. Excess hydrophobicity protein–ligand generates force along peptide backbone through hydrophobic effect. We describe mechanically strained structures involved aggregation determine transition between initial condensation polypeptide chains into ordered fibrillar structures. This is due excess attractive by within proteins assemblies. The process formation has mechanosensitive nature, significantly influences pathogenesis several neurodegenerative diseases.