Antibody Protein
I studied the antibody protein. Also known as immunoglobulins, antibodies are specialized cells of the immune system that work to prevent antigens from attacking the body. They work to detect foreign particles and fight it off to defend the body’s immune system. Using jolecule, I was able to see the specific arrangement of an antibody. Antibodies are Y shaped, and they are composed of two antigen binding sites. Each binding site has a heavy chain and a light chain. This variation allows the binding sites to vary from one antibody to the next. The following figures highlight some of the essential aspects of the protein.
Figure 1: Y Shaped Structure
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Figure 2: Constant Region
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Figure 3: Antigen Binding Site
Figure 1 shows the Y shaped structure of the antibody. This structure is beneficial because it can be modified so that the antibody can attach to the specific shape of the protein or sugar molecules attached to the antigen. Furthermore, figure 2 shows the constant region of the structure which functions to communicate with the other proteins in the immune system to determine how to get rid of the antigen. The ends of the heavy (green) chain and light (purple) chain are the constant regions of this structure. In contrast, the tips of the antibody (where the chain labels are in figure 1) represent the antigen binding site as depicted by figure 3. Figure 3 shows an overhead view of where the antigen binds to the chains. When binded, the immune system will be able to attack the antigen to protect the body.
Evidently, all three figures show the tertiary structure of the protein because the light chain and heavy chain are both apparent. To add, the polypeptide chains have folded into their functional shape. As a result, interactions between the chains allow for them to stabilize so that they can function efficiently. Essentially, the presence of both chains contribute to the function of the protein because both chains work together to attach to the antigen present so that it can, ultimately, be destroyed.
Do you happen to know any other proteins, beside the Antibody protein, that can defend the body's immune system through the detection of foreign particles? Also, how do the antigens bind to the chain? Is there something causing this bind or does it occur on its own?
ReplyDeleteThe only proteins I'm aware of that function to defend the body's immune system are antibodies. However, not all antibodies are the same so they are able to defend against a wide range of antigens. Well, the antigens have a either a sugar or protein molecule attached to them with a distinct shape to match the shape of the binding site on the chains.This allows the antigen to fit right into the binding site like a puzzle piece. Essentially, the immune system allows for binding to occur because it communicates with the protein to determine how to get rid of the foreign particle detected.
ReplyDeleteIn regards to the specific level of protein structure, can you further explain to why you thought the level of structure was tertiary?
ReplyDeleteThere were irregular shapes and folds, and there are only two chains labeled. Tertiary structures also have non polar molecules clustered towards the center, and I zoomed into the structure in jolecule and noted that there was a non polar region towards the center. Therefore, I reasoned that the level of protein structure was tertiary.
DeleteAre there specific antibodies that work to fight off different foreign structures?
ReplyDeleteYes, each antibody has a specific shape so that it can bind to specific foreign structures.
ReplyDeleteIs there a specific bonding site, like an amino acid chain, in which the antibody protein bonds to other proteins/sugars or is in different for each structure?
ReplyDeleteGood question. Well, as far as I know, the bonding site will always be located at the tips of the amino acid chains.
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