Infrared light-induced protein crystallization. Structuring of protein interfacial water and periodic self-assembly

In this experiment, it is demonstrated that applying low level non ionizing infrared radiation on proteins elicits mutual association and assembly of proteins, because IR radiation affects the interfacial water layers that are surrounding the protein, and separate the protein charge becoming a dipole macromolecule, being this what cause the association of proteins.

This can be related to the exclusion zones in water, as is mentioned in [1] applying infrared light on samples "significantly increased structuring of water associated with biopolymers and macromolecules" (there is a section [2] on EZ water on this web)

The authors also mention EZ waters, and they say that IR radiation structure water and accumulate more counter-ions around protein, where the structural correlations of water molecules aligned by the protein surface charges give rise to a hydration layer possessing a net dipole moment, dipole because macroions (proteins) have their inherently bound cloud of counterions (separated by a water medium).

They say that the protein nucleation is provoked because of "dipole-dipole" interactions, but refereeing only to electrostatic interactions, but in the web there are some papers proposing an electrodynamic (electromagnetic) interaction-recognition between macromolecules because of their dipolar nature. For example in [3] it can be read:

" .. dipole moments involved in the classical limit are due to conformational molecular vibrations. Since already three decades ago, experimental evidence is available regarding the existence of low-frequency excitations of macromolecules of biological relevance (proteins [5] and polynucleotides [6]) through the observation of the Raman and Far-Infrared spectra of polar molecules. These spectral features are commonly attributed to coherent collective oscillation modes of the whole molecule (protein or DNA) or of a substantial fraction of its atoms. These collective conformational vibrations bring about oscillations of the total electric dipole moment, suggesting that beyond all the well-known short-range forces, biomolecules could interact also at a long distance by means of electrodynamic forces, provided they undergo these collective excitations. We think of collective excitations as they a priori give rise to large dipole moments, they can be switched on and o by suitable environmental conditions, and, nally, because they can induce strong resonant dipole interactions between biomolecules when they oscillate at the same frequency or with the same pattern of frequencies. Resonance would thus result in selective forces."

We can always go upward or downward around the scale but always we found some potential or eventually proved electromagnetic frequency range that have a fundamental function.

[1] Santana-Blank, L., Rodríguez-Santana, E., & Santana-Rodríguez, K. E. (2013). Photobiomodulation of aqueous interfaces: finding evidence to support the exclusion zone in experimental and clinical studies. Photomedicine and laser surgery, 31(9), 461-462.

[2] EMMIND › Endogenous Fields & Mind › Water & Electromagnetic Fields › Electromagnetism & Water - Exclusion Zones

[3] Preto, J., Pettini, M., & Tuszynski, J. A. (2014). On the role of electrodynamic interactions in long-distance biomolecular recognition. arXiv preprint arXiv:1403.2477.

Last modified on 14-Mar-16

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