This steric self-intersection expels water from overlapping segments of the sheath and by Newton׳s second law moves the polypeptide chain in an opposite direction. When the total bend reaches 360°, the leading segment of water sheath intersects the trailing segment. Third, the force initiating the tertiary folding of proteins arises from twists at the position of each hydrophobic amino acid, that minimizes surface exposure of the hydrophobic amino acids and propagates along the protein. The newly recognized quantum force sharply bends the peptide and is part of a dynamic field determining the pathway of protein folding. This force results from quantum effects, appearing only when the system is within and interacts with an oscillating electromagnetic field. The surface of exposed hydrophobic amino acids is protected from water contact by small nanobubbles of dissolved atmospheric gases, 5 or 6 molecules on average, that vibrate, attracting even widely separated resonating nanobubbles. Structured water layers with both coherent and non-coherent domains, form a sheath around the new protein. Second, application of quantum field theory to water structure predicts the spontaneous formation of low density coherent units of fixed size that expel dissolved atmospheric gases. Forward motion ceases when the shape change or propelling force ceases.
Proteins emerging from the ribosome move and rotate without an external force if they change shape, forming and propagating helical structures that increases translocational efficiency. Molecular movement is instantaneous and size insensitive. First, moving water molecules obey the rules of low Reynolds number physics without an inertial component. The mechanism of protein folding during early stages of the process has three determinants.