For Proteins, Form Shapes Function Essay

Different types of bonds/interactions in proteins lead to different kinds of structures. Three of the most commonly known chemical bonds in proteins include the hydrogen bond, the covalent bond, and the ionic bond. In hydrogen bonds, hydrogen interacts with oxygen, nitrogen, or fluorine to form either the alpha helix, or the beta sheet, which in turn determines its secondary, tertiary, or quaternary structure. Another type of bonds, the covalent bond, links amino acids together by sharing electrons;

Haemoglobin is just one of the many possible forms and functions of a protein polymer. They all have different structures, which makes them specialised to carry out a particular function. For example enzymes. They are roughly spherical in shape due to the tight folding of the polypeptide chains. Enzymes play important roles in most biological processes, in particular metabolism and synthesis. The tertiary structure of an enzyme is of particular importance to its function and a slight change in the chain sequence and therefore it's shape can result in it becoming inactive. Enzymes work by combining with a substrate to form an enzyme-substrate complex, the substrate is then broken down and released. Each enzyme has a particular substrate that is can breakdown, this will be the substrate with the complimentary structure to that of the active site of the enzyme. For example starch is only broken down by amylase. As the shape of the active site depends on the shape of the polymer shape so does the over all function of the enzyme.

2. protein provide structure in every cell in our body- Proteins are present in all areas and processes of the cell. proteins hep maintain the cell keep its shape, and control the movement of particles in and out of the cell. It also help send signal and repair of damaged cells. Proteins control movement in the cell division.

Proteins are important for the human body. Proteins play many important roles in the body including the structure of enzymes; these are important proteins that help reactions occur in the body, such as releasing from the food we eat. Proteins also function as transport proteins such as hemoglobin; an iron

Proteins are the metabolic workhorses of the cell; they engage in a variety of essential activities ranging from enzymatically catabolizing macromolecular food sources to serving as structural components that maintain cell stability. Maximizing protein function relies on intricate non-covalent interactions occurring on the secondary, tertiary, and quaternary levels that help determine the overall shape of the protein. In their native states, proteins will assume the most energetically favorable configuration. Occasionally however, cells are exposed to exogenous disruptions such as heat stress. Heat Stress can compromise protein three-dimensional structure. Hydrophobic residues tend to be buried in the interior of the protein but when

3. Explain why the structure of a protein is important to how the protein functions. It’s important because it can make many complex shape and each shapes can have different functions.

Proteins are important as they help build muscles and help the body repair itself. Without protein we would probably be very weak. One way proteins help our body helps our bodies is that enzymes act as catalyst for chemical reactions in our bodies. This helps the body perform more efficiently. Antibodies are also proteins. These proteins help the body defend against infection. Proteins also act transport. They help bind atoms and molecules and transmit them throughout cells and the body. Proteins provide many uses to our body and are therefore important. We need

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.

The concept of protein domains and motifs has dominated the first half of this course. Discuss the relevance of protein domains to the following topics:

The Functions of Proteins Introduction Protein accounts for about three-fourths of the dry matter in human tissues other than fat and bone. It is a major structural component of hair, skin, nails, connective tissues, and body organs. It is required for practically every essential function in the body. Proteins are made from the following elements; carbon, hydrogen, oxygen, nitrogen and often sulphur and phosphorus.

Hemoglobin is composed of four protein chains, two alpha chains and two beta chains, each with a ring-like heme group containing an iron atom. The secondary structure of hemoglobin refers to the alpha helix and beta pleated coiling or folding of a polypeptide, this structure is a result of hydrogen bonding between different parts of the same amino acid backbone. An alpha chain consists of a polypeptide folding into a delicate coil that is held together by hydrogen bonds between every fourth amino acid. A beta chain consists of a side-by-side alignment of the amino acid chain. Two of each of these types of folding are present in the secondary structure.

The structure of a protein is determined by its primary, secondary and tertiary structure. The specific sequence of amino acids in a protein is known as its primary structure. The atoms within a chain are held together by covalent bonds. The polypeptide chain forms a backbone in proteins. Its secondary structure consists of several chains held in place by hydrogen bonds. The arrangement of a sequence of amino acids in polypeptides may be helical (α-helix) for

Bettelheim, Brown, Campbell and Farrell assert that polypeptide chains do not extend in straight lines but rather they fold in various ways and give rise to a large number of three-dimensional structures (594). This folding or conformation of amino acids in the localized regions of the polypeptide chains defines the secondary structure of proteins. The main force responsible for the secondary structure is the non-covalent

important role because every living organism needs proteins in order to speed up the biochemical

These new formations are held together by hydrogen bonds. The third level is the tertiary structure. The tertiary structure of a protein is a contorted secondary structure being twisted and folded all out of shape to form a 3-d complex. The type of bonding that holds these formations together are weak interactions such as hydrophilic, hydrophobic, ionic, and hydrogen bonds. These bonds are individually weak, but collectively strong. The forth level, which completes a protein, is quaternary structure, which occurs when two or more tertiary structures are joined together by polypeptide bonds.