Why do heavy metal salts denature proteins?

It complexes with organic matter and destroys the structure of organic matter, so it leads to denaturation.

According to the theory of coordination chemistry, the sulfhydryl group belongs to the soft base, and the heavy metal ions are mostly soft acids.

Yes. Heavy metals can form with proteins""Complexes", so heavy metal poisoning, can be detoxified by drinking milk.

Protein is a biological macromolecular compound, its internal structure is complex, and it is its complex spatial structure that determines that each different protein will have different properties. For example, most enzymes are proteins, and an amylase enzyme will break down starch because its spatial structure will react with starch and cause starch to decompose, which in a nutshell, that is, this amylase has the property of decomposing starch.

The heavy metal ions contained in the heavy metal salt will destroy the spatial structure of the protein, or it will also react chemically with the protein molecule to form a new spatial structure, that is, the "complex" mentioned in high school and college, which will destroy the original properties of the protein, so the heavy metal salt will denature the protein.

The principle of <> is that the heavy metal ions contained in the heavy metal salts will destroy the spatial structure of the protein, or it will also chemically react with the protein molecules to form a new spatial structure, which is the "complex" mentioned in high school and college, which will destroy the original properties of the protein and denature the protein.

Protein is a biological macromolecular compound, and its internal structure is very complex and complex, and it is its complex spatial structure that determines that each different protein will have different properties. For example, most of the enzymes are proteins, a type of amylase.

It will decompose starch because its spatial structure will react with starch and cause starch to decompose, which means that this amylase has the ability to decompose starch.

The principle of denaturing proteins by heavy metal salts is that the heavy metal ions contained in heavy metal salts will destroy the spatial structure of proteins, or it will also carry out chemical reactions with protein molecules, so that the difference will form a new spatial structure, that is, the "complex" mentioned in high school and college, which will destroy the original properties of the protein and denature the protein.

Protein is a biological macromolecular compound, and its internal structure is very complex, and it is its complex spatial structure that determines that each different protein will have different properties. For example, most enzymes are proteins, and an amylase enzyme will break down starch because it reacts with the starch in the pre-junction of the space, causing the starch to decompose, which means that this amylase has the property of decomposing starch.

According to the theory of coordination chemistry, the sulfhydryl group belongs to the soft base, and the heavy metal ions are mostly soft acids.

Protein denaturation must be caused by the destruction of its specific spatial conformation due to the action of some physical or chemical factors. Heavy metal ions denature proteins because heavy metal ions can form insoluble salts with the free carboxyl groups in proteins, which break some chemical bonds of proteins and destroy the spatial structure of proteins. So heavy metal ions denature proteins.

Heavy metal salts make proteins lose their physiological activity. Chemically called the denaturation of proteins, this process is irreversible.

Manifestations of proteins after denaturation.

a) Loss of biological activity.

The biological activity of proteins refers to the biological functions of proteins such as enzymes, hormones, toxins, antigens and antibodies, and the oxygen-carrying capacity of hemoglobin. Loss of biological activity is the main feature of protein denaturation. Sometimes only a slight change in the spatial structure of a protein can cause a loss of biological activity.

Protein molecules condense and precipitate out of solution.

2) Changes in certain physical and chemical properties.

After the denaturation of the protein, the physical and chemical properties change, such as the solubility decreases and the precipitation is generated, because some of the hydrophobic groups that were originally inside the molecule are exposed due to the loose structure, and the asymmetry of the molecule increases, so the viscosity increases and the diffusion coefficient decreases.

3) Changes in biochemical properties.

After protein denaturation, the molecular structure is loose, cannot form crystals, and is easily hydrolyzed by proteases. The denaturation of proteins is mainly due to the destruction of the structure inside the protein molecule. The spatial structure of native proteins is maintained by secondary bonds such as hydrogen bonds, and when the secondary bonds are broken after denaturation, the protein molecules change from an ordered and coiled tight structure to a disordered, loose stretch structure (but the primary structure does not change).

Therefore, the hydrophobic groups that were originally inside the molecule were exposed to a large number of molecules on the surface of the molecule, while the distribution of hydrophilic groups on the surface was relatively reduced, so that the protein particles could not be miscible with water and lost the water film, which could easily cause the collision between molecules and aggregate precipitation.

Well, it is not that the addition of light metal salts will dissolve, but that it should precipitate after adding saturated light metal salts, and the addition of unsaturated precipitation and dissolution are not necessarily, depending on the electrical properties. The addition of heavy metal salts will denature and precipitate.

The principle (I hope you can give me extra points, hehe) has two points.

There are two factors to ensure the dissolution of proteins, one is the solvation effect, that is, the solvation of various polar groups and water molecules of proteins, which has a promoting effect on dissolution. Another factor is the polar effect of the cavity, which is the equilibrium of protons gained or lost by protein molecules.

Generally, saturated salts are added, due to the action of ions on water molecules, which destroys the solvation effect, and also breaks the balance of electrons and protons, resulting in the precipitation of protein molecules, which is also the salting out.

Protein + soluble light metal salts will be salted out, + heavy metal salts will be denatured.

The peptide bonds in the protein are water-informed in the unsaturated salts, and salting out will occur in the saturated metallophilic salts.

Heavy metals refer to metals with a specific gravity greater than 5 (generally referring to metals with a density greater than 5). Heavy metals refer to metals with an atomic weight greater than 55. For example, the atomic weight of iron is 56, which is greater than 55, so it is also a heavy metal.

There are about 45 kinds of heavy metals, which are generally transitional elements. Such as copper, lead, zinc, iron, cobalt, nickel, manganese, cadmium, mercury, tungsten, molybdenum, gold, silver, etc.

Common heavy metal salts such as:

Copper sulfate, zinc sulfate, silver nitrate, mercury nitrate, lead nitrate, etc.

Factors that contribute to sex degeneration.

Physical factors: such as heating, ultrasonic, violent oscillation, rays, etc.

Chemical factors: ethanol and other organic solvents, strong acids, strong bases, heavy metal ions and alkaloid reagents.

Strong oxides. Substances that can be matched. As long as it can be changed in structure, it can be changed.