The Structure And Function Of Proteins And Enzymes Essay

The temperature can have a major impact on an enzyme. According to Campbell Biology author Reece etc. 2011 “The enzyme reaction will increase as the temperature increase with the increasing temperature….substrates collide with active sites more frequently when the molecules move rapidly.”(Reece etc 2011) Every enzyme hits its optimal temperature the reaction will be at its highest point.(Reece etc. 2011) When the

Temperature controls the speed the enzymes work at. Higher temperatures increase the kinetic energy which increases the chance of collision therefore speeding up the rate of

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These results show how temperature of extreme high, or low affects enzyme activity. The highest rate of enzyme activity occurred at 37 Cº. Anything that was hotter or cold than 37 Cº slowed the reaction rate. As I thought, 100 degrees would denature the enzyme, and that was the case. The data provided shows exactly what temperatures enzymes work best, and worst. The objective was achieved as we discovered the different reaction rates under different temperatures. The results are reliable, as we know enzymes do not work well when under extreme heat or denaturation occurs. What I learned in this experiment was that enzymes don’t work well under cold temperatures because they tend to move slower. My hypothesis did not quite match, because I thought they work best at lower temperatures.

However if the temperature exceeds the optimum temperature the enzyme becomes denatured. This is because there is too much energy causing the enzyme molecules to vibrate causing the bonds maintaining their tertiary structure to break. The enzyme unravels causing the shape of the active site to change so it can no longer fit with the substrate.

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

They are made up of amino acids (consists of amino group, carboxyl group, hydrogen atom, and R group). Polypeptide bonds form between amino acids to form polypeptide chains. Amino acid sequence is primary protein structure. The secondary structure is the bonding pattern of the amino acids (e.g. helix, sheet, etc.). The tertiary structure consists of the domain, where the sheets or helixes fold on each other and become stable. The quaternary structure consists of several polypeptide chains that form advanced proteins such as human leukocyte

The purpose of this lab is to discover how changes in temperature can affect enzyme activity. All walks of life, from humans to plants, are living because of biochemical reactions. Biochemical reactions are processes that occur on a cellular level and are responsible for sustaining life: Photosynthesis, Cellular Respiration, Digestion, etc. Within these reactions, molecules change their identity and transform into new molecules. In the middle of these molecular transformations are enzymes (sites.com).

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 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.

Enzymes are an important part of all metabolic reactions in the body. They are catalytic proteins, able to increase the rate of a reaction, without being consumed in the process of doing so (Campbell 96). This allows the enzyme to be used again in another reaction. Enzymes speed up reactions by lowering the activation energy, the energy needed to break the chemical bonds between reactants allowing them to combine with other substances and form products (Campbell 100). In this experiment the enzyme used was acid phosphates (ACP), and the substrate was p-nitrophenyl phosphate.

In most instances, protein molecules are usually embedded from hundreds to thousands of amino acids. A repertoire of twenty different amino acids, joined in any possible sequence allows the existence of an inconceivably large number of proteins that is infinite in nature.

Enzymes are macromolecules that act as a catalyst, and it’s a chemical agent that accelerates the reaction without being consumed by the feedback or the results (Campbell and Reece, 2005). After the adjustment by the enzymes, the chemical movement through the pathways of metabolism will become awfully crowded because many chemical reactions are taking a long time (Campbell and Reece, 2005). There are two kinds of reactions in nature. The first one is Catabolic reaction and the second one is Anabolic reaction. Catabolic reactions are large molecules that are broken up into smaller molecules (Ahmed, 2013). Anabolic reactions are small molecules that join to make larger molecules, like polymerization (Ahmed, 2013). If you

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.

Usually, the proteins are classified into one of the four structural classes such as, all-α, all-β, α+β, α/β. So far, several algorithms and efforts have been made to deal with this problem. There are two steps involved in predicting protein structural classes. They are, i) Protein feature representation and ii) Design of algorithm for classification. In earlier studies, the protein sequence features can be represented in different ways such as, Functional Domain Composition (Chou And Cai, 2004), Amino Acids