Proteins bind to transport proteins facilitating nucleus to cytoplasm transport.
Proteins can be associated with cytoplasmic receptor and chaperone proteins.
Protein molecules are imbedded in dipole water molecules that can take a clustered form.
Protein molecules undergo high-frequency spatial changes inducing vibratory conditions.
Unfolded (parts of) proteins adsorb (hydrated) cytoplasmic alkali cations like K+ and anions.
Cytoplasmic proteins bind organic compounds such as ATP and fatty acids.
Proteins are exposed to various force fields: electromagnetism, gravity, dark energy and zero-point energy.
Influence of force fields on protein structure is collected and integrated by 4D toroidal geometry.
Formation of functional 3-D proteins requires a combined genomic/electromic machinery.
Protein molecules undergo conformational changes that induce vibratory states.
Different protein molecules can show mutual specific coherent resonance patterns.
Proteins can communicate in functional networks through their resonant states.
Protein morphology is influenced by external electromagnetic and geo-magnetic fields.
Protein molecule folding is influenced by coherent macromolecular vibration domains in the cell.
Protein geometry can be modeled using space-time with 4 spatial dimensions.
Protein structure can, in principle, be modified by quantum entanglement as a long-distant aspect.