...Biochemistry Task 4 Bridget Paget 540146 June 18th, 2016 Enzymes are active proteins that are catalyst which speed up chemical reaction. Without these enzymes chemical reaction would be too slow for the body to benefit from. There are two important features that make all enzymes catalysts. First is the chemical reaction that speeds up or slows down, but remains unchanged. Secondly they increase rates without changing the chemical equilibrium between reactants and product. This allows the enzyme to move to the next substrate and the cycle starts over again. Gresham HS IB Biology. (2007) Wolfe,G.(2000) Fructose is almost completely metabolized in the liver. There are two steps of fructose metabolism. The first step to breakdown fructose is to split the substrate into fructose 1 phosphate. This is called fructokinase. The second step of fructose metabolism is that it undergoes hydrolysis of fructose 1 phosphate by aldolase B, which is an enzyme that breaks down into DHAP and glyceraldehyde. These products enter the glycolysis pathway where they are converted to pyruvate. Pyruvate is a necessary molecule for the production of ATP and the ...
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...Task 4: Metabolism 1. They speed up reactions and do not change themselves, which means they can be used over and over. Enzymes help facilitate chemical reactions. Enzymes will lower the activation energy needed to start the reaction and that is how the reaction will be sped up. Enzymes are specific for certain reactions and are proteins. Not all catalysts though are enzymes. (Sanders, 2014) 2. (Gresham HS IB Biology, 2007) 3. (Hudon-Miller, S. 2012) 4 & 5. When table sugar is consumed, it is broken down into glucose and fructose. Glucose is used in the blood stream. Glucose can be stored in the liver as glycogen. Fructose does enter glycolysis, but first two steps are original to fructose. The first step involves breaking down fructose into fructose-1 phosphate by the enzyme, fructokinase. Fructose is the substrate of fructokinase and it’s product is fructose-1 phosphate. Fructose-1 phosphate is converted into DHAP and glyceraldehyde (products), by the enzyme aldolase B which will enter the glycolysis pathway. (Hudon-Miller, S. 2012) In HFI, there is an aldolase deficiency, so there is no conversion of fructose-1 phosphate into DHAP and glyceraldehyde, so they do not enter the glycolysis pathway to produce ATP or in gluconeogenesis. The fructose is still achieving phosphorylation by fructokinase, which results in a build up of fructose-1 phosphate. The liver cells are unable to utilze fructose as energy. There becomes an abundant buildup of fructose-1...
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...BIOCHEMISTRY TASK 2 Running head: BIOCHEMISTRY TASK 2 1 A. BIOCHEMISTRY TASK 2 2 B. BIOCHEMISTRY TASK 2 3 C. BIOCHEMISTRY TASK 2 4 D. BIOCHEMISTRY TASK 2 5 E. The four forces that stabilize a protein’s structure at the tertiary level are as followed: Hydrophobic is the interaction between nonpolar amino acids (Borges, 2014). These amino acids are not capable of hydrogen bonding, however their hydrocarbon regions interact closely by pulling together tightly tucking away from the exterior of the cell (Borges, 2014). This is the weakest of bonds (Borges, 2014). Next, Hydrogen bonds are polar or charged amino acids (Borges, 2014). This is where one amino acid is sharing its hydrogen atom with another oxygen atom (Borges, 2014). This is a stronger bond than hydrophobic interaction but still weak (Borges, 2014). The third bond is called Ionic Bond...
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...Running head: BIOCHEMISTRY TASK 2 Biochemistry Task 2 Terry Buckman Western Governor's University Biochemistry Task 2 I want to talk about 4 of the bonds or interaction that stabilize a protein’s structure at the tertiary level. The first bond is the ionic bonding which is most sensitive to pH changes and can occur between oppositely charged R groups. The next one is disulfide bonds which are covalent bonds that can take place between two cysteine R groups. Another one is hydrophobic interactions which is nonpolar. These R groups will cluster together on the interior of the protein and this will minimize their contact with water. The last one is van der Waals interactions takes place between the tightly packed nonpolar R groups on the interior of the protein. I would like to talk about BSE or bovine spongiform encephalopathy, in other words mad cow disease. This disease is called by misfolding prions at the molecular level. There are harmful and nonharmful forms of prions. The nonharmful form is PrPc and the harmful form is PrPsc. The PrPsc are hydrophobic and will cause the normal proteins to conform to their misfolding and harmful prion shape. This happens by way of a chaperonin. A polypeptide chain will enter the chaperonin and with proper environment of chaperonin, the polypeptide chain will fold correctly and exit as the normal prion, PrPc. Now in BSE, a polypeptide chain will enter into a “bad” chaperonin, the prion, and will get a misfolded prion to exit, PrPsc...
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...Biochemistry Task 4 GRT1 208.5.4-01, 03-05, 5.5-02, 04-07 Western Governors University Biochemistry Task 4 GRT1 208.5.4-01, 03-05, 5.5-02, 04-07 A. Case 1: Hereditary Fructose Intolerance A1. Role of Enzymes in Processes Enzymes are proteins that carry out chemical reactions. They bind to substrates, which are basically substances that need to be broken down and changed into something else. When the enzyme and substrate bind, they form the enzyme-substrate complex. An enzyme will act in a specific way on the substrate that it is bound to in order to change it into a product, and at the end of the process, the enzyme is unchanged and ready to bind to the next substrate. An enzyme acts as a catalyst, something that lowers the energy required to complete a chemical reaction (activation energy) without itself being changed. (Hudon-Miller, 2012) In the case of fructose breakdown, an enzyme called fructokinase is responsible for splitting fructose into fructose 1-phosphate, a six-carbon fructose. Another enzyme called aldolase B splits fructose 1-phosphate into two three-carbon molecules, dihydroxyacetone phosphate (DHAP) and glyceraldehyde. These products are then able to enter the glycolysis pathway to be converted to pyruvate, which is essential for the citric acid cycle and the production of adenosine triphosphate (ATP) for cellular energy. A2. Deficiency in Aldolase B A hereditary deficiency in aldolase B could be caused by mutations in the ALDOB gene. An aldolase...
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.... Biochemistry Task 4 GRT1 208.5.4-01, 03-05, 5.5-02, 04-07 Western Governors University Biochemistry Task 4 GRT1 208.5.4-01, 03-05, 5.5-02, 04-07 A. Case 1: Hereditary Fructose Intolerance A1. Role of Enzymes in Processes Enzymes are proteins that carry out chemical reactions. They bind to substrates, which are basically substances that need to be broken down and changed into something else. When the enzyme and substrate bind, they form the enzyme-substrate complex. An enzyme will act in a specific way on the substrate that it is bound to in order to change it into a product, and at the end of the process, the enzyme is unchanged and ready to bind to the next substrate. An enzyme acts as a catalyst, something that lowers the energy required to complete a chemical reaction (activation energy) without itself being changed. (Hudon-Miller, 2012) In the case of fructose breakdown, an enzyme called fructokinase is responsible for splitting fructose into fructose 1-phosphate, a six-carbon fructose. Another enzyme called aldolase B splits fructose 1-phosphate into two three-carbon molecules, dihydroxyacetone phosphate (DHAP) and glyceraldehyde. These products are then able to enter the glycolysis pathway to be converted to pyruvate, which is essential for the citric acid cycle and the production of adenosine triphosphate (ATP) for cellular energy. A2. Deficiency in Aldolase B A hereditary deficiency in aldolase B could be caused by mutations in the ALDOB gene. An...
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...This document is designed to help you organize your task as you work through the cohort. Please make a copy of this document, which will then appear in your Google Drive. (See below.) If you would like a tutorial on using Google Drive, please click here. Then insert your work into the copied document as instructed. We recommend you do your work in black, and delete all of the blue text prior to submitting your task. When your document is ready to go, save it as a PDF. You can upload this PDF to Taskstream and submit! Protein Structure A. Insert your original model of an essential amino acid that shows all atoms and bonds in both the backbone and the side chain. Click here to learn how to insert images into a Google Document. (Insert in-text citation here). 1 Characteristics of Leucine: Hydrophobic Oxygenation Insert your description of two characteristics (e.g., reactivity, hydrophobicity, how it affects the structure or functions of a protein) for the amino acid model you created in part A. (Insert in-text citation here). B. Insert your original diagram, or series of original diagrams, of the different levels of protein structure. 1. Check to see that you labeled the primary, secondary, tertiary, and quaternary structures in your diagram(s). Primary Secondary Tertiary quaterrnary (Insert in-text citation here). C. Insert your original diagram, or series...
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...Task 4 Western Governors University Biochemistry C624 November 9, 2015 A1. Describe two important features that make all enzymes catalysts. An enzyme is a protein that serves as catalysts of biological reactions converting a substrate into a product. The catalyst can increase the rate of the reaction. A catalyst does not change, or get consumed, during the reaction. A2. Create an original diagram, or series of diagrams with clear labels depicting the enzymatic cycle (lock and key or induced fit model). A3. Create a diagram that illustrates the aE of a reaction in the presence and absence of an enzyme. A4. Explain the reactions catalyzed by enzymes in the first two steps of fructose metabolism in the liver. Fructose in the blood passes through the cell membrane into the liver cell and initiates phosphoralation with fructokinase for the metabolism of fructose. The fructokinase then uses the phosphate and produces F-1-P (fructose 1 phosphate). F-1-P is the substrate for the enzyme Aldolase B. Aldolase B takes the F-1-P and makes DHAP and glyceraldehyde, the products of Aldolase B. The DHAP and glyceraldehyde are intermediates in glycolysis and continue down to make pyruvate which then can make ATP synthesis or fatty acids. (Sanders, J. 2013) A5. Discuss how a deficiency in aldolase B is responsible for HFI. Hereditary Fructose Intolerance (HFI) results from a deficiency of aldolase B activity primarily in the liver, but also in the kidneys and small intestine...
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...GRT task 2: Biochemistry (V. Undergrad-0814) Proteins are made up of smaller units called amino acids. Hundreds or thousands of amino acids in long chains form a protein molecule. There are 20 different types of amino acids that combine to make a protein. Amino acids are classified into three groups: essential amino acids, non-essential amino acids, and conditional amino acids. Essential amino acids cannot be made by the body and must come from food. Non-essential amino acids can be produced by the body even if not obtained through food ingested (Wolfe,2000). Conditional amino acids are needed at times of stress, like an illness. Proteins can be described as polar and non-polar depending on how they interact in the environment. Polar and non-polar chemical trait allows for the amino acid to direct themselves toward water (hydrophilic) or away from water (hydrophobic). Valine is an essential amino acid that enables chemical messages to be transmitted from the brain. Valine’s chemical structure is C5H11NO2 and is a branched chain amino acid. Valine is non-polar in nature so it is not a charged molecule. Valine is hydrophobic and if found deep inside the structure for this reason. Valine is important to muscle function as the muscle recovers from strenuous activity. The amino acids sequencing of a protein decides its structure and function. Protein function is also dependent on its structure but some changes can disrupt the structure. When a protein loses function it...
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...Biochemistry Task 3 Sandy Palma 457307 October 26, 2015 A. 1. Explain differences between the oxygenated and deoxygenated states of two hemoglobin. With Oxygenated blood the heme has a plantar shape as for Deoxygenated the heme is domed, cooperativity causes the shape. Another difference is color. Heme is bright red when bound to oxygen, as for deoxygentaed blood the heme is purple to bluish in color. 2. Explain how pH impacts the binding and release of oxygen by hemoglobin CO2 in the blood creates a decrease in pH, this causes the hemoglobin to release their oxygen molecules. A decrease in CO2 causes the pH to increase, which causes the hemoglobin to pick more oxygen molecules. A. 3. Hudon-Miller, S. (2012) HudonMiller, S. (2012) 1. 2. 3. Explain how diseased cells differ from normal red blood cells in their capacity to transport oxygen. They differ by its shape. Normal red blood cells are concave disk shape. The diseased cell has a sickled shape. The sickled shape causes the cells to get stuck in the blood vessels, thus preventing them from bringing oxygen to other parts of the body. 4. a. Identify the type of inheritance seen in sickle cell anemia. The trait is inherited when hemoglobin S is obtained from one parent with the trait and a normal hemoglobin parent. Sickle cell disease is inherited when both parents have the trait or the disease . b. SOURCES...
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...Jessi Ayers 11-8-2015 Biochemistry Task #3 1. Explain two differences between the oxygenated and deoxygenated states of hemoglobin. One big difference would be that the oxygenated state of hemoglobin has oxygen binding to the heme portion of the molecule. Deoxygenated hemoglobin has released the oxygen to the tissues. Hemoglobin has two states; Taut and relaxed. Deoxygenated hemoglobin is in the “T” state and Oxygenated hemoglobin is in the “R” state. Deoxygenated hemoglobin has a low affinity for oxygen in its “T” state, while Oxygenated hemoglobin binds with greater affinity. 2. Explain how pH impacts the binding and release of oxygen by hemoglobin. The way pH acts and binds and releases oxygen is called the, “Bohr effect.” The ability of hemoglobin to bind to oxygen is related to CO2 concentration. CO2 concentration is also directly related to acidity; the more CO2, the higher the acidity, which also means a lower pH level (Low pH equals high acidity). When the CO2 concentration gets higher and the pH gets lower, it causes the hemoglobin to “get rid” of the oxygen. On the flip side, when there is less CO2 and the pH increases, this causes the hemoglobin to “pick up” the oxygen. This process is also known as the, “Hemoglobin Dissociation Curve.” 3. Explain how the diseased cells differ from normal red blood cells in their capacity to transport oxygen. Normal red blood cells contain hemoglobin that assist in transporting oxygen to the whole body, referred to as...
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...International Institute of Management 1 Hospital Management System CERTIFICATE This is to certify that Hospital Management System embodies the original work done by Mansi Chitkara, Namita Khandelwal, and Avinash Chaporkar during this project submission as a partial fulfillment of the requirement for the System Design Project of Masters of Computer Application IV Semester, of the Rajasthan Technical University, Kota. Swati V. Chande Principal (MCA Department) International School of Informatics and Management Mrs. Kapila Pareek Assistant Professor International School of Informatics and Management 2 Hospital Management System ACKNOWLEDGEMENT The satisfaction that accompanies that the successful completion of any task would be incomplete without the mention of people whose ceaseless cooperation made it possible, whose constant guidance and encouragement crown all efforts with success. We are grateful to our project guide Mrs. Kapila Pareek for the guidance, inspiration and constructive suggestions that helpful us in the preparation of this project. We also thank our colleagues who have helped in successful completion of the project. Mansi Chitkara Namita Khandelwal Avinash Chaporkar 3 Hospital Management System CONTENTS 1. Introduction 1.1 Purpose 1.2 Scope 1.3 Technologies used 1.4 Overview 2. Overall Description 2.1 Goals of Proposed System 2.2 Background 2.3 Project Requirements 2.4 User Characteristics 2.5 Constraints 2.6 Definition of...
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...Biochemistry: Task 5 Christi Corder 000356780 November 1, 2015 A. There are three sources of fatty acids in the body. One of these sources is adipose tissue, in which adipose tissues release tissue fatty acids. Another source is the liver, which makes fatty acids, which travel through the bloodstream. Dietary fat is also a source. Three stages are involved in the breakdown of fatty acids to produce ATP. These are beta oxidation, the citric acid cycle, and the electron transport chain. A fatty acid is a long chain of carbons and hydrogens with a carboxylic acid group at the end. In beta oxidation, the fatty acid is broken down into two carbon units, which produce acetyl-CoA, and electrons and hydrogens are removed. The first step of beta oxidation occurs when the fatty acid is activated by the addition of a CoA subunit and the fatty acid is broken down into carbon units called acetyl-CoA and electrons and hydrogens are removed. The electrons and hydrogens are carried by NADH and FADH-2 to the electron transport chain and are used to make ATP. NADH and FADH-2 are also produced during the CAC and these also enter the electron transport chain and are used to produce ATP from ADP and inorganic phosphate. Also, the hydrogens from NADH and FADH-2 combine with oxygen and the electrons to form water. (O’malley, 2014). B. One difference between saturated and unsaturated fatty acids is that saturated fatty acids have as many hydrogens as can possibly fit around the...
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...Western Governors University Biochemistry 10/16/2015 Task 1 Diagram 1: Showing the beginning of the DNA replication process Diagram 2: Showing the leading and lagging strand and the direction they replicate. Also showing Okazaki Fragments, and the 3” to 5” end of DNA. The arrows in the above diagram show the 3” to 5” direction that the DNA replicates; starting in the origin of replication and moving towards the 5 direction, using Okazaki fragments in the Lagging strand. Diagram 3: Showing a more detailed version of DNA replication. Showing the enzymes that assist in transcription. Diagram 4: Showing how mRNA assists in the transcription and translation process. Diagram 5: Showing the roles of tRNA and ribosomes during translation. Diagram 6: Showing how transcription takes place inside the nucleus and the translation takes place in the cytoplasm of the cell. Diagram 7: A detailed diagram showing protein translation. Showing how the DNA coding strand is matched by the mRNA. RNA is a multifaceted molecule. “RNA is an intermediary, carrying genetic information from the DNA to the machinery of protein synthesis” (Goodsell, 2003). The enzyme RNA polymerase creates different RNA molecules. RNA polymerase is made up of several proteins and they work together to surround DNA strands, unravel them and build an RNA strand based on the information inside the DNA. RNA polymerase needs to be accurate in its copying of genetic information and its production...
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...! ! ! ! ! ! Western Governors University Biochemistry GRT Task 5: Lipids, The Importance of Fat in the Diet ! ! ! ! ! ! ! ! ! Melissa Robinson Student ID: 000389892 mrobi70@wgu.edu June 2015 Fat is often maligned in the media, and is often named “public enemy #1” because of the obesity epidemic that our country has been struggling against for several years. However, fat is an essential component in the human body. Fat must be taken in and used by the body to maintain health. That said, moderation is key. Too much of a good thing, can lead to other health issues, as seen by the obesity level in this country. It is important to strike a balance between healthy consumption of fats that the body needs to function, and the other end of the spectrum, too much fat or no fat at all in the diet. Below is a brief overview of how the body uses fats, known as lipids, in the body and why lipids are essential to the body’s health. A. Energy Stored as Fat Food is often shared with others socially and enjoyed for its taste and aroma. Fatty foods are often considered pleasurable to eat because they provide people with richness of flavor, texture and an overall feeling of satisfaction. However, fat in foods is not just there for pleasure. The body uses fat an energy source. The fat is stored in tissue called “adipose tissue.” A special type of molecule, called a triglyceride, is used by the body to store fat. Triglycerides are used as large, fat storage...
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