Ÿ Proteins bind to transport proteins facilitating nucleus to cytoplasm transport.

Ÿ Proteins can be associated with cytoplasmic receptor and chaperone proteins.

Ÿ Protein molecules are imbedded in dipole water molecules that can take a clustered form.

Ÿ Protein molecules undergo high-frequency spatial changes inducing vibratory conditions.

Ÿ Unfolded (parts of) proteins adsorb (hydrated) cytoplasmic alkali cations like K⁺ and anions.

Ÿ Cytoplasmic proteins bind organic compounds such as ATP and fatty acids.

Ÿ Proteins are exposed to various force fields: electromagnetism, gravity, dark energy and zero-point energy.

Ÿ Influence of force fields on protein structure is collected and integrated by 4D toroidal geometry.

Ÿ Formation of functional 3-D proteins requires a combined genomic/electromic machinery.

Ÿ Protein molecules undergo conformational changes that induce vibratory states.

Ÿ Different protein molecules can show mutual specific coherent resonance patterns.

Ÿ Proteins can communicate in functional networks through their resonant states.

Ÿ Protein morphology is influenced by external electromagnetic and geo-magnetic fields.

Ÿ Protein molecule folding is influenced by coherent macromolecular vibration domains in the cell.

Ÿ Protein geometry can be modeled using space-time with 4 spatial dimensions.

Ÿ Protein structure can, in principle, be modified by quantum entanglement as a long-distant aspect.