Structure Waves in Biological Systems: Evidence for deBroglie Waves in Protein Crystals -Summary
John Grant Watterson
18 Tomanbil Terrace, Ashmore, 4214, Australia
(retired: formerly, Department of Science Griffith University, Southport, 4217, Australia)
email: [email protected]
Keywords: water clusters, structure wave, proteins, α helix, β sheet
Submitted: January 31, 2024
Revised: January 5, 2025
Accepted: February 10, 2025
Published: March 12, 2025
1. Abstract
The cluster model of liquid structure explains the origin of the forces that are responsible for osmotic phenomena. In contrast to the many textbook explanations based on thermal motion of solute molecules, the model, based on coherent co-operative motion of solvent molecules (water), is shown to explain also other hydration mechanisms, including protein function. Its central concept, the pressure pixel, is defined as the volume occupied by a molecule in a perfect gas (about 40 cubic nm at ambient conditions), which is assumed to be the smallest volume in which pressure is exerted in liquids also. The collision mechanism of the familiar kinetic theory of gases is replaced by co-ordinated motion of molecules of solution propagating as a structure wave. It is shown how, when clusters of different solutions in contact carry and exchange equal energies (kT), cluster size, as judged by wavelength, is predicted to be in the 1 nm size range and obey the deBroglie relation. In addition, it is emphasized that long-standing results from X-ray, electron and neutron scattering give the fundamental protein domain size also in this range. This physical property indicates that both water clusters and protein domains, support the same wave motion. It is further concluded that oscillation of the H-bonded internal structures of domains must therefore also be periodic, with α-helices performing longitudinal and β-sheets performing transverse motion in synch with the structure wave of the whole medium.