>As I posted previously NaCl is essentially incompatible with H2O because their component atoms have entirely different orbital electron rings in terms of their radial parameters between which repulsion occurs. However, the radial parameter of non-bonded three electron rings in the outermost electron shell of Cl atom and two non-bonded electron rings in the outermost electron shell of oxygen atom are nearly the same. So that a large number of water molecules can associate linearly around Cl atom of NaCl due to Meissoner's magnetic attraction between Cl and O. Thus NaCl molecules are possible to be compatible with water molecules.
It is not limited to understand dissolution phenomenon of inorganic
materials but also all kind of organic substances. Dr, Yoon explains
how raw egg-white can dissolve into water despite that it has a long
chain conformation of proteins, and turns into gel that looks white
when boiled up to 70 degrees C. He explains amino acids building
egg-white protein are connected with -CO-NH- segments upon which a
large number of water molecules are attached by a linear association,
as such CO*OH2*H2O*OH2*H2O*......., and NH*H2O*OH2*H2O*...... Here
symbol * reveals Meissoner's magnetic attraction.
He defines these water chains associated linearly by Meissoner's
magnetism as bio-waters in living organic tissues. So that protein
chains with such a long dimension can readily dissolve in water and
possible to coexist with water molecules. It is as though caffeine and
nicotine molecules can dissolve in a critical phase of CO2 to build a
gas/solid solution system.
Biochemistry today explaining this dissolution of egg-white into
water, attributes to protein chains to fold to form a globular
conformation. However, it is quite wrong. In polymer science it is
common knowledge polymers with a globular conformation have the lowest
viscosity compared with that having linear one. So the protein molecule
of egg-white must have a linear conformation because it has the highest
When we heat the egg-white up to 70 degrees C, or mechanically agitate
it, the bio-water chains associated on CONH segments of protein chains
being stripped off, and the bare protein chains that are inherently
hydrophobic have to precipitate out and aggregate by themselves to
build a network structure to form a gel phase. Thus liberated water
molecules from the association of bio-water in raw egg-white turn out
to pack in the networks of protein chains as tiny droplets which
scatter the incoming light white.
However, the polymer chains from which water chains are stripped off,
never redissolve into their initial water solvent. it is because the
space between aggregated protein chains does not allow to rebuild up
bio-water chains, due to a stronger packing attraction between them.
Likewise silk fibrin protein attaching bio-waters on their CO-NH
segments are contained in silk worm body. When this aqueous silk fibrin
is discharged as filaments, it builds silk fibers evaporating water
from them, but they never redissolve into the original same water
solvent. Thus this kind of worms can build their own cocoons possible
to protect their pupas from rains and external enemy attack. How
wonderful is the intelligent design of fiber forming protein polymers
and water solvent that dissolve them and spin out as native silk for
these living things!
Dr. Yoon proved indirectly the existence of solvent chains built by
linear association of dimethyle acetamide, which link between CONH
segments of aromatic polyamide to form a gel crystal. And he could
confirm that once these solvent chains are stripped off from the CONH
segments of polymer chains, these polymer chains never redissolve into
the original dimethylacetamide solvent. He wrote this in his Nature