How the Structure of Proteins Are Related to Their Function

The protein molecules in many foods provide the amino acid building blocks required by our own cells to produce new proteins. To determine whether a sample contains protein, a reagent called Biuret solution is used. Biuret solution contains copper ions. However, the chemical state of the copper ions in Biuret solution causes them to form a chemical complex with the peptide bonds between amino acids (when present), changing the color of the solution. Biuret solution is normally blue, but changes to pink when short peptides are present and to violet when long polypeptides are present.

Proteins are the basis of the protoplasm (fluid living content of the cell that contains the cytoplasm and cell nucleus) and are found in all living organisms. Proteins make up the bulk of animals body’s non-skeletal structure. As enzymes, they catalyze biochemical reactions; as antibodies, they prevent the effects of invading organisms; and as hormones, they control metabolic processes (C. Bissonnette, 2011). The Biuret test was used to detect the presence of peptide bonds within proteins, and they were found present in test tube #9 (control for peptide bonds).

Each gene acts as a code, or set of instructions, for making a particular protein. They tell the cell what to do, give its characteristics, and determine the way its body works. Each protein has a unique sequence of amino acids. This means that the number and order of amino acids is different for each type of protein. The proteins fold into different shapes. The different shapes and sequences give the proteins different functions, e.g. keratin are a fibrous protein found in hair and nails. If the gene has even the slightest of disorder within its sequence it could lead to an inaccurate order of amino acids

The functional groups are called aminos and carboxyls. The linkage type is by using a peptide bond. The primary function of protein is build and repairs the body.

Among human beings, Sickle-Cell Anemia is a particularly well-studied example of adaptation. This chapter teaches me that Sickle-Cell Anemia is a painful disease in which oxygen-carrying red blood cells change shape and clog the finest parts of the circulatory system (page 57). Sickle- Cell changes their shape from the usual discs to shrunken sickle shapes. These sickle shaped red blood cell gives the disease its name. This type of disease is caused by a genetic mutation in a single base of the hemoglobin genes (page 58). It is considered that this disease is the result of when two abnormal Hemoglobin, a protein in red blood cells that passed down from parents to child as an autosomal recessive pattern. I don't not know anyone personally with

A protein has multiple existing structures, these are the primary, secondary, tertiary and quaternary structures which occur progressively. A protein is essentially a sequence of amino acids which are bonded adjacently, and interact with one another in various ways depending on the R group that the amino acid contains. There are 20 different amino acids which are able to be arranged in any given order, thus giving rise to a potential 2.433x1018 (4.s.f) different combinations, and therefore interactions between the various amino acids.

Proteins are complex structures made up of chains of amino acids. Each protein has a different function such as enzymes to catalyze reactions or protein hormones to trigger certain functions of a cell. First let’s start with the most basic component of a protein: an amino acid. An amino acid is made up of a central carbon atom attached to a hydrogen atom, a carboxyl group, an amino group, and an R group which varies

The amino acids bond together in bonds called peptide bonds. A chain of amino acids is called a polypeptide chain. The structure in which the amino acids are bonded determines the function of the protein. There are about twenty different amino acids, but there is a wide variety of possible combinations that amino acids can bond, therefore proteins have quite a lot of functions. Some things proteins are used for are the building of the muscles, tendons, organs, glands, nails, and hair. There are many more different functions for proteins. To detect proteins in test materials, there is an identifying agent called Biuret Solution which when mixed with the test material. It turns purple if it contains a protein. The darker the violet color, the more concentrated it is with protein.

The disease is caused by a mutated version of the gene that help makes hemoglobin. Hemoglobin is the protein that carries oxygen in red blood cells. Sickle cell is a disorder in the blood caused by abnormal hemoglobin proteins. The abnormal hemoglobin protein caused sickle cell shaped red blood cells. The sickle cell red blood cells are crescent shapes and can clog up very easily in blood canals. In the diagram to the right it shows how a mutation causes a change in the amino acid.

Proteins are polymeric chains that are built from monomers called amino acids. All structural and functional properties of proteins derive from the chemical properties of the polypeptide chain. There are four levels of protein structural organization: primary, secondary, tertiary, and quaternary. Primary structure is defined as the linear sequence of amino acids in a polypeptide chain. The secondary structure refers to certain regular geometric figures of the chain. Tertiary structure results from long-range contacts within the chain. The quaternary structure is the organization of protein subunits, or two or more independent polypeptide chains.

A genetic disorder caused by the abnormal gene for hemoglobin S is called sickle cell anemia. Only replace that take place in glutamic acid is to fill in for valine as the sixth codon of the hemoglobin protein, which alter declines the hemoglobin’s ability transform oxygen throughout your body. The human body needs oxygen in order to function when we eat food and liquid for energy even including muscles, repairs our cells, feeds our brain, breath and nerves. Normal cells are described as round, red, flexible and travel easily throughout your blood vessels. Sickle cell anemia describes a red blood cell that has inflexible, tacky, and create like a crescent moons not like the normal red cells. It tends to slow down or block the blood flows while

Sickle-cell disease majorly affects the hemoglobin that is present in our blood. The job of hemoglobin is to help transport oxygen and carbon dioxide to and from the cells throughout our body. Hemoglobin is present specifically in our red blood cells. Each red blood cell contains two hundred and eighty million hemoglobin molecules. Red blood cells normal shape is a biconcave shape because of the lack of many organelles and a nucleus. The shape is so important to a red blood cells functioning that if it is not shaped normally it has major consequences. The shape helps them to fit through capillaries easier and also allows for an increased surface area which results in easier gas exchange. Sickle-cell disease is a genetic disease that causes issues in the oxygen/carbon dioxide carrying hemoglobin molecules that are present in our red blood cells.

Normal red blood cells and sickle diseased cells differ in their capacity to deliver oxygen in a few important ways. One difference is each cell's respective flexibility. Normal red blood cells are flexible and are able to move through small and large vessels. Once sickle cells have deoxygenated the cell becomes rigid, sticky and form long fibers due to stacking on one another. This fibers then force the cell to sickle. Every cell may not be the sickle or crescent shaped but will be irregularly shaped. These shapes and the cell's inability to flex prevent them from maneuvering in and out of small vessels, therefore preventing the tissues to receive the oxygen they need. The diseased cells also become stick and tend to stack on each other.

Campbell and Farrell define proteins as polymers of amino acids that have been covalently joined through peptide bonds to form amino acid chains (61). A short amino acid chain comprising of thirty amino acids forms a peptide, and a longer chain of amino acids forms a polypeptide or a protein. Each of the amino acids making up a protein, has a fundamental design that comprises of a central carbon or alpha carbon that is bonded to a hydrogen element, an amino grouping, a carboxyl grouping, and a unique side chain or the R-group (Campbell and Farrell 61).

B) Proteins Proteins are made up of chains of amino acids. Each protein folds into a characteristic three dimensional shape that is essential to its function. They perform a variety of functions in cells and are probably the most diverse macromolecule in living systems. The Biuret test detects the presence of proteins and short peptides (short chains of amino acids). Biuret reagent contains a strong solution of sodium hydroxide (NaOH) and a very small amount of dilute copper sulfate solution. The reagent changes color in the presence of a protein because the amino groups in the amino acids react with the copper ions producing a violet color. A negative result is blue.