The stabilizing factor of protein solution is that the hydration layer on the surface of protein molecules can prevent the aggregation of protein molecules and charged protein molecules, which repel each other with the same charge . Relevant discussions are as follows:
1. First, the hydration layer on the surface of protein molecules can prevent the aggregation of protein molecules. This is due to the relationship between water molecules. the hydration layer and protein molecules There is an attractive force which ensures the stability of the protein molecule.
2. Second, protein molecules are charged and the same charges will repel each other, which allows the protein molecules to maintain a certain distance in solution and avoid aggregation. These two factors work together to allow protein solutions to remain stable under certain conditions.
The interaction between protein molecules in aqueous solution is as follows:
1. Hydrogen Bonds: In protein molecules, the side chains of amino acids and the backbones of the peptide chain There are hydrogen bonds between them. The formation of hydrogen bonds is mainly due to the interaction between N, H and O, N, S and other atoms. This interaction helps maintain the three-dimensional structure of the protein.
2. Van der Waals Forces: Van der Waals forces between protein molecules include induction forces, dispersion forces, and orientation forces. These forces play a role in protein folding and conformation maintenance.
3. Hydrophobic Interactions: Hydrophobic interactions within and between protein molecules are crucial for maintaining the three-dimensional conformation and quaternary structure of proteins. Thishe interaction mainly involves interactions between amino acid side chains and membrane lipid molecules.
4. Electrostatic Interactions: Protein molecules are charged, so electrostatic interactions between molecules are very important for protein conformation and function. This interaction mainly involves interactions between amino acid side chains and polar ions and molecules.
5. Coordination interaction: In some proteins, metal ions or ligands coordinate with amino acid residues in the protein, which helps maintain the conformation and catalytic activity of the protein.
6. The synergistic effect of Van der Waals forces and hydrophobic interactions: Van der Waals forces and hydrophobic interactions have a synergistic effect in maintaining protein conformation. When hydrop interactionshobes bring protein molecules together, Van der Waals forces help to strengthen this aggregation, and vice versa.
Biology has not solved the problem September 19: 3. Different organic molecules have different binding capacities (hydrophilicity) with water molecules
It binds water. The amino and hydroxyl groups at the end of the peptide chain can form hydrogen bonds with the bound water.
The activity of a protein is linked to its specific site (such as the catalytic center of an enzyme), and exposure of this site requires stability of the protein's spatial conformation, otherwise changes in space. The structure can lead to coverage of the site of action. The protein loses its activity. Bound water can stabilize protein conformation.
Next, you want to ask why proteins are more hydrophilic than starch.
Polarity of the protein surfacePresence of groups and charged groups makes it easily hydrophilic. This positive and negative charge is formed by the ionization of the amino and carboxyl groups. Therefore, the surface of proteins consists of charged areas and hydrophilic areas formed by unevenly distributed charged groups. Hydration layer around proteins There is a hydration layer around protein molecules that is tightly or weakly bound to the protein molecules. The tightly bound hydration layer can reach 0.359/g protein, while the loosely bound hydration layer can reach more than 2 times the molecular mass of the protein.