Christian Nordqvisit Essay
Christian Nordqvisit does a good job of explaining proteins by comparing them to machines, machines that make all living things. Proteins are the building blocks of life they make up what we are, how we function, how we fight off a cold, they are a part of every function throughout our bodies. Proteins are constructed from a set of 20 amino acids, each amino acid has a common core structure and a side chain. The core is made up of 3 different components a hydrogen atom, an amino functional group, and a carboxyl functional group. The core is the same in all 20 amino acids, but the side chain makes each amino acid different. There are four different types of side chains acidic, basic, uncharged polar, and nonpolar. These different amino acids link together
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These are known as the immunoglobulins and for short we will use Ig. The five main antibodies are IgA, IgM, IgE, IgD, and IgG, this document focuses mainly on the IgG immunoglobulin. Let’s first look at what the five immunoglobulins do. The IgA immunoglobulin protects body surfaces exposed to the outside, so this would be your skin, the body’s first defender. IgM immunoglobulins which are the largest in size of all the immunoglobulins, are the first antibodies made in response to infection. The IgE immunoglobulins are involved heavily in people with allergies, they react to certain allergens in the air. The IgD immunoglobulins are found in the tissues that line the belly or chest, and their function is unclear. Last we have the IgG immunoglobulins and they are the smallest in size yet most abundant in the body. They are very important in fighting viral and bacterial infections. Figure 3 shows each class of immunoglobulin and what they look like. When looking at the antibodies we see that the IgG, IgE, and IgD all have the same structure with little difference. The difference is in the hinge which will be discussed in greater detail
These are known as the immunoglobulins and for short we will use Ig. The five main antibodies are IgA, IgM, IgE, IgD, and IgG, this document focuses mainly on the IgG immunoglobulin. Let’s first look at what the five immunoglobulins do. The IgA immunoglobulin protects body surfaces exposed to the outside, so this would be your skin, the body’s first defender. IgM immunoglobulins which are the largest in size of all the immunoglobulins, are the first antibodies made in response to infection. The IgE immunoglobulins are involved heavily in people with allergies, they react to certain allergens in the air. The IgD immunoglobulins are found in the tissues that line the belly or chest, and their function is unclear. Last we have the IgG immunoglobulins and they are the smallest in size yet most abundant in the body. They are very important in fighting viral and bacterial infections. Figure 3 shows each class of immunoglobulin and what they look like. When looking at the antibodies we see that the IgG, IgE, and IgD all have the same structure with little difference. The difference is in the hinge which will be discussed in greater detail