Differential Scanning Calorimetry ( Dsc )

Temperature is a measure of kinetic energy. As this movement increases, collision rate and intensity, and therefore reaction rates, increase. This experiment was conducted to determine if there is a minimum temperature that increase kinetic energy and denature enzymes to slow enzymatic reactions or fail to catalyze them. The experimental results indicate an increase in temperature will increase reaction rates until proteins denature.

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

The chaperones have the main role of ensuring proper folding. When a chaperone protein becomes toxic, major changes in the conformation occur as the alpha helix becomes beta pleated sheets. The sheets now expose the hydrophobic amino acid and aggregation, or clumping together of sheets occurs (Borges, 2014).

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.

their normal shape to an abnormal shape, however, the chemical composition of the protein remains

The basic building blocks of proteins are amino acids, the biuret reaction tests for protein. A solution of sodium hydroxide is added to a sample then a few drops of copper sulphate solution, if positive – the solution will turn mauve. There are 20 different amino acids and they can be joined in any order. Therefore there can be many different functions. A protein consists of one or more polypeptide chains (a polypeptide chain being multiple amino acids joined together via condensation, producing a peptide bond). Different proteins have different shapes as the shapes are determined by the sequence of amino acids.

The structure of an enzyme as protein has a primary, secondary, tertiary, and sometimes quaternary structure. The primary structure of an enzyme, like any protein, is the order of its amino acids. The secondary structure involves alpha helices and beta pleated sheets. Alpha helices are a coil that is formed by hydrogen bonding between every fourth amino acid. Beta pleated sheets are formed by hydrogen bonding between two or more parts of the polypeptide chain that are side by side. The tertiary structure contains disulfide bridges, ionic bonds, hydrophobic interactions, and hydrogen bonds. Disulfide bridges are the result of two sulfhydryl groups interacting because the the folding of the protein. Ionic bonds can form between polar groups on amino acids. Hydrophobic interactions are the cluster of amino acids with nonpolar side chains that is commonly seen in proteins. Hydrogen bonds can also form. The quaternary structure of an enzyme is when multiple proteins are bonded together in one complex made of proteins subunits.

The temperature is the measure of the average kinetic energy of the reacting particles. The increase in temperature also changes the distribution of molecular kinetic energies.

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.

This folding describes the arrangement of the amino acids. The shape of the acids is held in place by the hydrogen bonds. A hydrogen bond is a dipole-dipole interaction between a hydrogen atom and an electronegative atom. The hydrogen bonds are important because if they didn’t hold the structure of the amino acids in place, there would be no backbone for the protein.

They are key constituents of all biological systems, and perform a great variety of functional and structural roles. Proteins play a crucial role in almost all biological processes, like signal transmission, catalysis, and structural support. This important range of functions comes from the existence of thousands of proteins, which are each folded into a characteristics three-dimensional structure, the same structure that allows it to interact with one or perhaps more molecules. A lot of the functional and structural studies of proteins are conducted with purified preparations of proteins. In general the purification methods of proteins aim to exploit the differences in their different properties such as, solubility, size, charge, and resin-binding specificity, all with the purpose to enrich the solution for the targeted protein

This technique could be used when a chemist discovers a compound. The chemist could use the digimelt to melt the compound and to identify the melting point. The chemist could thencompare the melting of the compound to a list of compounds. This helps the chemist to identifywhat compound he found. One way to improve this lab would be to test all the equipment and make sure it works beforeusing it.

The purpose for this experiment is to determine if different proteins denature, physically change, at the same temperature. By doing this, we can prove that not all proteins are made the same, and that they have different structures.

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).

It is capable of operating at 300ºC with around 70% heat recovery capability. They are used where cross contamination between gas streams must be prevented in applications such as ovens and steam boilers.