What is the affinity of antibodies?
Antibodies are molecules that circulate around the body within the immune system. These molecules are individually designed to bind to specific foreign substances known as antigens. Individual antigens have specific shapes and chemical makeup, so antibodies have specifically shaped binding areas to match the antigen. The strength of the binding between the antigen and the binding point on the antibody is called the affinity of the antibody. In general, the stronger the affinity, the more effective the antibody can be recognized by the attacker.
Every biological organism or part of the organism consists of organic molecules. The arrangement and the amount of these molecules is specific to the body. For example, a bacterial cell has a structural cell membrane that has different molecules in which each makes a specific job. Some may bind to environmental substances to bring them to the cell while other external molecules can help attach the bacteria to the Ahosting cell during the INVAfrom the host.
The human body has developed a system of cells and molecules that half the body and control the attackers. Antibodies are not cells, but rather molecules that hover around, waiting for the attackers or pieces of attackers. The antibody population consists of a wide range of molecules, each specially structured to fit on a specific type of molecule, such as external molecules on the outer bacterial cell. After the body is exposed to pathogen, such as the measles virus and can clean the infection, it has a memory of the type of antigens present on the virus and creates specialized antibodies specifically to combat other pathogen infection.
These specialized antibodies have a specific shape in their binding areas that fit perfectly into the antigens of viral particles. The power of the connection between one binding point of the antibody to one antigen on the attacker is known as the affinity of the antibody tothe bonding place. Looking at more than one binding point on the antibody is the strength of the binding between the places and the attacker known as the avidity or functional affinity of the antibody.
Their simplest antibodies and antigens are collections of atoms that are held together with chemical ties. The type of bonds that hold the antigen on the antibody are of unpleasant links, which means that individual atoms and molecules do not share any of their electron particles, but rather hold together through forces such as weak electrical attractions. Normally, there are bonds that do not include the movement of electrons from one molecule to another, relatively weak, but a collection of many innocent bonds can be strong. This situation occurs in the interactions of antibodies and antigen and is the basis for the affinity of antibodies.
AFFINITY Power of antibodies is important for effective identification of attackers and subsequent infection. Vaccines tend to produce strong affinity antibodies to their antigens because antigenY are derived specifically from the target pathogen and created to be very recognizable. Despite the advantages of the strong affinity of the antibody, however, the body is able to benefit from the weak affinity of antibodies, as these can allow the body to recognize new attackers that are somehow similar to previously recognized attackers.