Protein interaction methods

Protein is an extremely important substance. It is an indispensable substance in the process of life. Protein is broken down into more refined nutrients such as sugars through the digestive system in the body, providing the body with a continuous supply of energy. There are many types of proteins, and different proteins can interact with each other. Let’s take a look at how proteins interact with each other.

The experimental methods for studying DNA-protein interactions mainly include: a. gel retardation experiment; b. DNase1 footprint experiment; c. methylation interference experiment; d. in vivo footprint experiment; f. pull-down experiment. New technologies recently used to study protein/nucleic acid interactions include: nucleic acid aptamer technology, bioinformatics methods, protein chip technology, and nanotechnology.

Interactions of protein molecules:

1. Interaction of biological macromolecules: Three conditions required for biological macromolecules to exert their physiological functions: molecular structure, molecular movement and change, and interaction between molecules.

1. Non-covalent bonds: ionic bonds, hydrogen bonds, van der Waals forces and hydrophobic bonds. The transmission and utilization of information relies heavily on weak non-covalent bonds. They determine not only the three-dimensional structure of biological macromolecules, but also how these structures interact with other structures.

2. Characteristics of the force: molecular binding and dissociation

2. Protein-protein interaction Structural mode of interaction between proteins: the interaction occurs through the protein's motif, element or domain.

3. DNA-protein interaction: the chemical bonds between the two

1. Hydrogen bond: The helical structure of proteins with recognition function often interacts with the major groove of DNA.

2. Hydrophobic bond: The T-CH3 group exposed to the side source of the major groove is hydrophobic and can interact with the side chains of hydrophobic amino acid residues.

3. Ionic bonds Proteins are also biological macromolecules, with hydrogen bonds, van der Waals forces and hydrophobic bonds. The existence of these forces makes proteins more stable.