...energetic collisions When molecules collide, the kinetic energy of the molecules can be converted into chemical potential energy of the molecules. If the chemical potential energy of the molecules become great enough, the activation energy of a exergonic reaction can be achieved and a change in chemical state will result. Thus the greater the kinetic energy of the molecules in a system, the greater is the resulting chemical potential energy when two molecules collide. As the temperature of a system is increased it is possible that more molecules per unit time will reach the activation energy. Thus the rate of the reaction may increase. 2) The number of collisions per unit time will increase. In order to convert substrate into product, enzymes must collide with and bind to the substrate at the active site. Increasing the temperature of a system will increase the number of collisions of enzyne and substrate per unit time. Thus, within limits, the rate of the reaction will increse. 3) The heat of the molecules in the system will increase. As the temperatue of the system is increased, the internal energy of the molecules in the system will increase. The internal energy of the molecules may include the translational energy, vibrational energy and rotational energy of the molecules, the energy involved in chemical bonding of the molecules as well as the energy involved in nonbonding interactions. Some of this heat may be...
Words: 384 - Pages: 2
...* Key Topics: * Explain and give examples of why proteins are essential to cell function * The basic structure of an amino acid * Describe the 4 levels of protein structure, and give examples of each * Explain what an enzyme is, understand why enzymes are needed to help chemical reactions, and know the role of the active site * Revisiting the Theory of Chemical Evolution * Modern life arose through a series of endergonic chemical reactions. 1. Production of small organic compounds * i.e., formaldehyde (H2CO), hydrogen cyanide (HCN) 2. Formation of mid-sized molecules from these small compounds * i.e., amino acids, simple sugars 3. Mid-sized building blocks combine to form large molecules. * i.e., proteins, complex carbohydrates 4. Life became possible when one of these large molecules self-replicated. * Organic Molecules * Large organic molecules are called macromolecules * Four major categories of macromolecules: 1. Proteins 2. Nucleic Acids 3. Carbohydrates 4. Lipids * Several of these are long chains of smaller subunits. * The smaller subunits are known as monomers * The long chains of monomers are known as polymers * Four groups of Macromolecules * Building Macromolecules – Monomers and Polymers * Molecules, such as amino acids, are individual units called monomers. They link together (polymerize) to form polymers, such as proteins...
Words: 1630 - Pages: 7
...Introduction Enzymes are biological catalysts. Catalysts are substances that increase the rate of chemical reactions without being used up themselves. Enzymes are also proteins. They all have different and complex shapes that allow smaller molecules to fit into them. The place where these substrate molecules fit is called the active site. The shape of an enzyme can change; its active site may no longer work. It is said the enzyme is denatured. They can be denatured by high temperatures or extremes of pH. Like all other proteins, enzymes are made of amino acids. Each enzyme is made of between 100 to 1 million amino acids placed like pearls on a string. Each amino acid is bonded to the next by chemical bonds. Some enzymes can be made from 20 different kinds of amino acids. No two enzymes are alike. Each enzyme has its own unique sequence of amino acids, which is determined by the genes in the cells. Enzymes consist of millions of amino acids placed one after the other, however, do not look like a long string of amino acids. In most enzymes the string is coiled and folded thousands of times to form a highly complex three-dimensional structure. It is the chemical interactions between the amino acids that force the enzymes into their three-dimensional structure, which is held together by the many different links between the different amino acids. Each enzyme has its own unique three-dimensional structure that determines the function of the enzyme. The three-dimensional structure of enzymes...
Words: 960 - Pages: 4
...March 12th 2010 2.1.18 Enzymes are Globular Proteins Catalyst Molecule/element that speeds up a chemical reaction but is not used up in the reaction and remains unchanged after the reaction Globular proteins have specific tertiary structures. The shape comes from the protein’s primary structure (Sequence of amino acids) and it’s secondary structure. In globular proteins the tertiary structure usually has hydrophobic R groups in the centre and hydrophilic R groups around the outside of the ball. Enzymes are: Globular proteins and soluble in water Able to break molecules down or build them up! Biological catalysts Specific- because they catalyse a reaction with only one type of substrate Their globular structure has a pocket called an active site Activity affected by temperature and pH (Rate of reaction) Enzymes are large molecules with hundreds of amino acids. A lot of these amino acids work to keep the specific tertiary structure of the enzyme. The function of the enzyme depends on the shape, and for the enzyme to work correctly the tertiary structure must be maintained specifically. All of the structures (primary, secondary, tertiary) of the enzyme is involved in the specific active site shape. (Where the catalytic activity of the enzyme happens) Enzymes are faster than catalysts and because they are specific to one reaction they do not produce unwanted by products. An individual cell could contain over one thousand enzymes to catalyse every process, like digestion, respiration...
Words: 351 - Pages: 2
...Enzymes and pH pH is a measure of H+ concentration. The higher the concentration of H+ the lower the pH values (acids) A hydrogen ion has a (+) charge so will be attracted to negatively charged molecules or parts of molecules. As like charges repel, positive molecules or parts of molecules will repel hydrogen ions. Large numbers of hydrogen bonds and ionic bonds are responsible for holding the tertiary structure of an enzyme protein in place. This ensures that the active site is also held in the right place. These bonds are due to the attraction between oppositely charged groups on the amino acids that make up the enzyme protein. Because of their charge, hydrogen ions can interfere with the hydrogen and ionic bonds in the molecule holding the tertiary structure in place. This means increasing or decreasing the concentration of hydrogen ions can alter the shape of the tertiary structure and therefore the shape of the active site. This can also aler the rate of an enzyme-controlled reaction. The induced-fit hypothesis suggests that an important part of catalysis in the active site relies on charged groups on the R-groups of the amino acids that make up the active site. Increasing the concentration of hydrogen bonds will alter the charges around the active site, as more hydrogen ions are attracted towards any negatively charged groups in the active site. Optimum pH At the optimum pH, the concentration of hydrogen ions in the solution gives the tertiary structure...
Words: 595 - Pages: 3
...Describe how inhibitors affect the rate of an enzyme-catalysed reaction Describe the advantages of using immobilised enzymes in industrial processes * Two types of inhibitors – Competitive and non-competitive * Both types of inhibitors reduce the rate of reaction * Competitive inhibitor is structurally similar and competes with substrate for active site of enzyme * This prevents substrate from binding to the active site * Fewer/ no enzyme-substrate complexes formed * If substrate concentration is increased in reduces the effect of the inhibitor. * Non-Competitive inhibitor binds away from the active site * This alters the overall shape of the enzyme, including active site * Substrate and inhibitor are not competing for the same active site * Therefore increasing substrate concentration will have no effect of rate of reaction * Enzymes tolerate wider range of conditions such as temperature/ph * Enzymes are easily reused thus reducing costs * Several enzymes can be used together * Product is not contaminated * Enzymes are easily added or removed Describe the functions and importance of mitosis to living organism using example where appropriate Describe how meiosis differs from mitosis and explain the significance of these differences * Mitosis results in daughter cells that are genetically identical * That have the same...
Words: 951 - Pages: 4
...Enzymes are proteins produced by a living organism, and act as efficient catalysts for specific chemical reactions. They are able to convert a specific set of reactants, known as substrates, into a specific set of products. Even at low temperatures, enzymes continue to allow a reaction to occur by lowering the activation energy of the given reaction. Reactions continue to occur even in the absence of enzymes, however due to the slow reaction rates without enzymes, sometimes the effects of the reaction would be considered insignificant. Enzymes are present in all aspects of plant metabolism, with their most important role in being the reduction of oxidative stress caused by photosynthesis and cellular respiration. These processes produce superoxide radicals, such as the anion O2-, which is a highly toxic by-product of metabolism within plant chloroplasts. The anion becomes no longer toxic with the use of the enzyme superoxide dismutase, which...
Words: 436 - Pages: 2
...PO43− or a related anion or a group such as —OPO(OH)2 * Adenine – A * Guanine – G * Cytosine – C * Thymine - T * Adenine – A * Guanine – G * Cytosine – C * Thymine - T Deoxyribose Deoxyribose Main idea 2: The structure of DNA is a double helix. It was discovered through the work of several scientists. Hydrogen bonds play important roles in the secondary, tertiary, and quaternary structures of proteins. (In alpha helices and beta sheets, the three dimensional, folded structure of the protein, and the joining together of subunits of the protein). In DNA, H bonds hold together the two strands. This attraction is weak enough so that the strands can be pulled apart in replication and transcription. Hydrogen bonds play important roles in the secondary, tertiary, and quaternary structures of proteins. (In alpha helices and beta sheets, the three dimensional, folded structure of the protein, and the joining together of subunits of the protein). In DNA, H bonds hold together the two strands. This attraction is weak enough so that the strands can be pulled apart in replication and transcription. C C A pair of parallel helices intertwined about a common axis, especially that in the structure of the DNA molecule. A pair of parallel helices intertwined about a common axis,...
Words: 796 - Pages: 4
...for energy (for both storing and supplying energy), and in some cases can be used structurally, such as cellulose Lipids H O H H C H H C H H C O C O O C O O These come in many varieties: fats, oils, cholesterol, steroids, and more, and have uses in cellular membranes, insulating and protecting, and also act as a minor energy supply C H Proteins Proteins have several uses, such as for transport and structure; but they are also the basic components of all enzymes, hormones, antibodies, haemoglobin, ribosomes, and many more materials Water H O H Another essential life component, this is the most important content of many reactions forming most of these molecules, and also metabolic reactions; water is also an essential structural component in plants, and in the diet of animals Nucleic acids These are responsible for the formation of both DNA and all forms of RNA molecules, consisting of individual nucleotides www.asbiology101.wordpress.com Enzymes These are proteins which are used in many reactions – their function is to catalyse metabolic reactions in the vast majority of living organisms There is a lot of chemistry knowledge in the Biological Molecules section of this module, which is why it is important that you are aware of a few chemistry basics, such as the types of chemical bond. This unit on Biological Molecules is centred...
Words: 21136 - Pages: 85
...INTRODUCTION: Lipase also called as triacylglycerol acylhydrolaseis an enzyme known for its enormous applications for industry and diagnostics. Their basic activity is to convert fats into fatty acids and glycerol. These enzymes are water soluble in nature. They also convert polar solvents into more lipolytic substances. In 1856, a scientist name claude Bernard has identified lipase [1]. Lipases are serine hydrolases containing G-X1-S-X2-G sequences as the catalytic part of the particle, where G = glycine, S = serine, X1 = histidine, X2 = glutaminic or aspartic acid. Such structure is characteristic also for serine proteases. The knowledge of their 3-dimensional structure plays a significant role in designing and structuring lipases...
Words: 875 - Pages: 4
...mammalian cells and Plant cells and reduce the binding capacity of the plant glycosylation enzyme. 2.2 SECONDARY OBJECTIVE : To predict the differences in the antigenicity of HPV 16 L1 gene expressed in recombinant mammalian cells and Plant cells. 3. LITERATURE REVIEW Markéta Šmídková et al.,(1998) mentioned in “Plant Production of Vaccine Against HPV: A New Perspectives”, the considerations of post translational modifications in therapeutic vaccine production including differences in glycosylation between plant and mammalian systems which gave us a basis for our work. Michael Karbiener et al,.(2004) “Humanization of the N-glycosylation pathway in plants and plant production systems” states the need to prevent addition of immunogenic N-glycans as this could induce IgE binding and rapid immune clearance of plant glycosylated therapeutics when injected into a mammal. Hence we chose 3 specific glycosylating enzymes to modify by mutation. Chandrasekaran et al in their work et al,. (2008) “Isolation and properties of alpha-D-mannose: beta-1,2-N-acetylglucosaminyltransferase from trachea mucosa” stated in detail the properties of the N acetyl glucosaminyl transferase enzyme including its specificity to terminal-branched mannosyl residues of glycoproteins. We used this information in our docking studies between the enzyme and the L1 protein. Margaret Stanley...
Words: 945 - Pages: 4
...Effects of Temperature, pH, Enzyme Concentration , and Substrate Concentration on Catecholase Introduction Enzymes are biological proteins that speed up the reaction rate of a chemical reaction. They work in the human body by lowering activation energy making certain that reactions will initiate. For every action, there is an equal and opposite reaction. In this case, factors that influence the activity of an enzyme are called modulators. If modulators activate enzymes the reaction rate catalyzed will significantly increase, but if the modulator inactivates enzymes the reaction rate catalyzed will significantly decreased (Silverthorn, 2004). The potentially disastrous influence of temperature, pH, enzyme concentration, and substrate concentration on enzymes and other proteins is one reason why these modulators are very strictly regulated by the body (Silverthorn, 2004). Temperature, a measure of the intensity of heat, is an important factor in the activity of enzymes. The velocity of an enzymatic reaction is influenced by temperature. This is because substrates collide with active sites frequently in the presence of rapidly moving molecules. In addition, although these molecules do move rapidly the speed of the reaction drops sharply. In short, thermal agitation causes protein molecules (enzymes) to denature ( breakdown of protein structures). All enzymes have an optimal temperature at which reaction rates go fastest without denaturing the enzyme (Campbell and Reece, 2002) pH...
Words: 1991 - Pages: 8
...Unit 15 Biochemistry of Health Check list for Health P1 describe the structure of hydrogen, carbon, oxygen and nitrogen and relate these to the structure of biological molecules. Use diagrams to describe the atomic structure of hydrogen, oxygen and nitrogen. Use diagrams to describe biological molecules (glucose, amino acids, fatty acid). Explain how hydrogen, oxygen and nitrogen combine to form the biological molecules. P2 describe the structure of water and carbon dioxide with reference to different types of bonding. Use diagrams to describe the structure of water and carbon dioxide. Describe the type of bonds within the molecules of water and carbon dioxide. P3 describe the structure and function of organic molecules. Use diagrams to describe the structure of glucose, amino acids and fatty acids. Explain the functions of glucose, amino acids and fatty acids. P4 explain the processes of aerobic and anaerobic respiration. What is aerobic respiration? What is anaerobic respiration? Include the equations of aerobic and anaerobic respiration. P5 demonstrate the factors that affect enzyme activity. Use graphs to demonstrate these factors that affect enzyme activities: Temperature, pH, Concentration, Substrate concentration and enzyme concentration. P6 explain the causes of different types of metabolic disorders. Give examples of inherited metabolic diseases. ( WebMD.com) M1 explain the relevance...
Words: 381 - Pages: 2
...diagnosis is made when the presence of HIV is confirmed and the CD4 count drops below 200 cells/mL or after an AIDS indicator condition is diagnosed. Regimens of antiviral drugs can slow the immune system deterioriation in infected patients and extend the life expectancy of those who have developed AIDS. The most common serotype is HIV-1 which is distributed worldwide The RNA viruses which are retroviruses enters CD4 cells by binding to a specialized site which is receptor on a body cell. Then, the virus loses its protective coat and releases RNA, its genetic material , and an enzyme known as reverse transcriptase . The enzyme reverse transcriptase contained inside the viral core to convert their RNA into a form that can enter the host cell’s nucleus and incorporated with the cell’s genetic material. Hence , it build DNA strands based on the RNA strand and it is shown in figure 1.1 in 3-D structure in cartoons display which is taken from RasMol. This reaction happens at in the polymerase active site, which is formed by two sets of arms that surround the RNA and DNA. The polymerase site is shown in figure 1.2 which is...
Words: 1558 - Pages: 7
...Introduction & Hypothesis: Enzymes are important for every living organism, because they are the reason that reactions occur. Although most reactions would take place without enzymes, enzymes allow these chemical reactions to happen at a much faster rate, therefore making cells more efficient (Reece, 2011). Enzymes are catalysts, and almost always proteins, that speed up the rates of reactions by lowering the activation energy without being consumed in the reaction (Helms, 1998). Throughout this experiment, four procedures will be performed to indicate the factors that alter the functioning of enzymes, and the importance that these factors are to be in correct levels in order for a cell to function properly. Proteins are macromolecules with unique polypeptide chains that make up their structure (Reece, 2011). The functions of proteins are dependent on their structure, and since enzymes are almost always proteins, the structure of the enzyme is very important for the enzyme to function. However, there are factors that can disrupt the structures of enzymes. These can be environmental factors such as temperature and pH, or they can be concentration changes, such as an increase or decrease in enzyme or substrate concentration (Eed, 2013). Temperature is an environmental factor that can alter enzyme activity (Reece, 2011). An increase in the kinetic energy of a solution results in an increase in temperature (Reece, 2011). As the temperature increases, the molecules in the...
Words: 2657 - Pages: 11
