Author(s)

Dirk K. F. Meijer^1*, Hans J. H. Geesink²

¹University of Groningen, Groningen, The Netherlands.
²Biophysics Group, Loon op Zand, The Netherlands.

The current geometric and thermodynamic approaches in protein folding studies do not provide a definite solution to understanding mechanisms of folding of biological proteins. A major problem is that the protein is first synthesized as a linear molecule that subsequently must reach its native configuration in an extremely short time. Hydrophobicity-hydrophilicity models and random search mechanism cannot explain folding to the 3-D functional form in less than 1 second, as it occurs in the intact cell. We propose an integral approach, based on the embedding of proteins in the whole cellular context under the postulate: a life protein is never alone. In this concept the protein molecule is influenced by various long and short distance force fields of nature such as coherent electromagnetic waves and zero-point energy. In particular, the role of solitons is reviewed in relation to a novel GM-scale biophysical principle, revealed by us. This recent finding of a set of discrete EM frequency bands, that either promote or endanger life conditions, could be a key in further studies directed at the morphogenetic aspects of protein folding in a biological evolutionary context. In addition, an alternative hypothesis is presented in which each individual cell may store integral 3-D information holographically at the virtual border of a 4-D hypersphere that surrounds each living cell, providing a field receptive memory structure that is instrumental in guiding the folding process towards coherently oscillating protein networks that are crucial for cell survival.

Protein Folding, Coherent Wave Pattern, Electromagnetic Fields, Solitons, Harmonics, Cellular Automata, Quantum Mechanics

Meijer, D. and Geesink, H. (2018) Guided Folding of Life’s Proteins in Integrate Cells with Holographic Memory and GM-Biophysical Steering. Open Journal of Biophysics, 8, 117-154. doi: 10.4236/ojbiphy.2018.83010.