...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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...Biochemistry Task 2 October 17, 2015 (Yatherajam, 2015) (Yatherajam, 2015) Organic Compounds. Retrieved October 16, 2015, from http://legacy.owensboro.kctcs.edu/gcaplan/anat/Notes/API Notes D organic chem.htm Polypeptides (n.d.) Retrieved October 16, 2015, from http://www.sparknotes.com/testprep/books/sat2/biology/chapter5section5.rhtml Pepsin Enzyme: Structure, Function, and Important Facts. (2014, September 25). Retrieved October 16, 2015, from http://www.buzzle.com/articles/pepsin-enzyme-structure-function-and-important-facts.html There are four forces, both bonds and interactions, which help stabilize or hold together a tertiary structure. These four forces include hydrophobic interactions, hydrogen bonds, ionic bonds, and disulfide bonds. Hydrophobic interactions are the weakest of the four forces and they occur between nonpolar amino acids. According to Borges (2014) these hydrophobic interactions occur in amino acids such as leucine and phenylalanine. The amino acids involved in hydrophobic interactions are amino acids which are not capable of hydrogen bonding. The next force is hydrogen bonding, which occurs between polar or charged amino acids like tyrosine and aspartate, according to Borges (2014). At the oxygen level the amino acids share their hydrogen atom with one another, one hydrogen atom becomes the donor and the other the recipient. The hydrogen bond is stronger that...
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...Biochemistry Task 2 Brandy McDowell 000499302 November 30, 2015 A. (Lyman, 2013) B. (Wolfe, 2000) (Wolfe, 2000) B. (Wolfe, 2000) (Wolfe, 2000) C. (Hudon-Miller, 2012) D. (Hudon-Miller, 2012) E. The four forces that stabilize a protein. * Hydrophobic interactions which are interactions by nonpolar amino acids. The weakest of the four types of bonds. * Hydrogen bond made up of interactions of polar or charged amino acids. The amino acids share their hydrogen. This is also a weak bond, but it is stronger than the hydrophobic interaction. * Ionic bonds are made up of charged amino acids. A positive charge of an amino acid attracts to a negative charge of another amino acid. This bond is a little stronger than the hydrogen bond, but not as strong as the polypeptide bond. * Disulfide bond only occurs between two cysteine amino acids. Two cysteine amino acids form a sulfa-sulfa bridge. This is a strong covalent interaction. (Borges, 2014) F1. Explain the role of prions in BSE, including each of the following: ●How prions are formed – Prions are malformed proteins. Instead of reproducing, the prions cause normal proteins to change to the malformed version. The normal prion (PrPc) is bound to the surface of neurons. PrPc can be altered and become misfolded taking on a different conformation which is then known as PrPsc. ●The connection between misfolding and aggregation – Because the misfolded prions are hydrophobic...
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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 4 Western Governors University September 14, 2015 Running head: BIOCHEMISTRY TASK 4 1 A1. Enzymes increase the rate of a chemical reaction without being altered in the process of the reaction (HudonMiller, 2013). Enzymes also lower activation energy without altering the chemical reaction or products (HudonMiller, 2013). A2. BIOCHEMISTRY TASK 4 2 A3. A4. Fructose metabolism has two steps different steps in the liver, the substrate of fructose breaks down to fructose1phosphate by an enzyme called fructokinase; fructose1phosphate is turned into DHAP + glyceraldehyde by an enzyme known as aldolase B, DHAP +glyceraldehyde BIOCHEMISTRY TASK 4 3 A4 continue then enters glycolysis, glycolysis turns into pyruvate goes through citric acid cycle and produces ATP (HudonMiller, 2013). BIOCHEMISTRY TASK 4 5 A5. In hereditary fructose intolerance there is an aldolase B (which is the enzyme for the substrate fructose1phosphate) can no longer take its substrate fructose1phosphate and turn it ...
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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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...Heather Mandigo Biochemistry task 2 Student ID #000598641 BIOCHEMISTRY TASK 2 2 A. (Yatherajam, 2015) B. (Wolfe, 2000) (Khan Academy, 2016) B. (Khan Academy, 2016) C & D. (Hudon-Miller, 2012) E. The four forces that stabilize the protein structure at the tertiary level are hydrophobic interactions, ionic bonding, disulfide bridges and hydrogen bonds (Wolfe, 2000) Hydrophobic interactions occur when the amino acids have a R group that is hydrophobic/nonpolar (Wolfe, 2000). These hydrophobic groups migrate to the inside of the molecule since they are rejected by water (Wolfe, 2000). These hydrophobic molecules are water fearing. Ionic bonding occurs when the R group is charged and there is an attraction between positive and negative charges (Wolfe, 2000). Disulfide bridges occur between 2 cysteine molecules and only occurs between these 2 molecules (Wolfe, 2000). These types of bonds have very strong covalent bonds (Wolfe, 2000). Hydrogen bonds occur between R groups that are polar or charged (Borges, 2014). What happens is, a hydrogen atom is shared with another amino acid between a nitrogen atom or an oxygen atom, creating the hydrogen bond (Borges, 2014). These are the weakest of the bonds (Borges, 2014). F. Prions play a significant role in the development of bovine spongiform encephalopathy or Mad Cow Disease. Prions are proteins which cause disease (Wolfe...
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...Biochemistry Task 5- Lipids Student ID# Western Governors University 05/21/2015 Biochemistry Task 5- Lipids A. Fat is stored in the body and used as an energy source when not enough energy is available from food. This process involves dismantling the stored fat in fat cells and releasing the components into the bloodstream. The major storage form of fats in our body are triglycerides, which are made up of three fatty acids bound to glycerol. Adipocytes are primary cells that store fat in the triglyceride form. White adipose cells are used to store energy (O’Malley, M. 2014). 1. Triglycerides are the storage molecules that are broken down and used to produce ATP. The triglycerides break down into two different items, glycerol and fatty acids. The triglycerides are formed when glycerol binds to three fatty acid molecules. The fatty acids each break down into 2 carbon parts. Each part of the carbon makes Acetyl CoA. The Acetyl CoA molecule then enters the Citric Acid Cycle before it moves on to the next step, the electron transport chain. The end result of each of these steps is the production of 12 ATP (Hudon-Miller, 2012). B. 1. Saturated fats do not contain a carbon-carbon double bond. Unsaturated fats contain at least on carbon-carbon double bond. The saturated fatty acid chains can stack while the unsaturated fatty acid chains are kinked by the double bond. 2. Saturated fats have a high melting point and are solid at room temperature...
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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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...Nancy Bosch Task 2 Student #000514178 Task 2: Protein Structure A. ("Amino Acids") B. (Rafael) (Wolfe) (Rafael) C. (Wolfe) D. (Wolfe) E. Explain the four forces (i.e., bonds or interactions) that stabilize a protein’s structure at the tertiary level. Hydrophobic interactions- R group in the amino acid is non-polar and therefore will avoid contact with water by joining together in the interior of the molecule, it will avoid contact with water. Van der Waals- this interaction occurs when the hydrophobic R groups that are packed together have a weak attraction that helps to reinforce the hydrophobic bond. Ionic bonding- The R group must have a charge. In this case the opposites attract (positive to negative/ negative to positive) forming a very strong bond.Disulfide bridges- These bonds are formed with the help of cysteine. One of the sulfur atoms from cysteine forms a single covalent bond with a second sulfur atom from another cycsteine located in the protein chain. (Wolfe) F. Explain how bovine spongiform encephalopathy (BSE) occurs at a molecular level by doing the following: 1. Explain the role of prions in BSE, including each of the following: ● how prions are formed A prion is a protein that causes infection. They are formed when a mutation occurs. A normal prion protein called PrPc is found in our neurons in our brains. This normal protein gets altered and becomes a PrPsc protein which then binds to another normal PrPc...
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...Biochemistry Task 2 Ashlyn Verrecchio 000502421 October 13, 2015 Requirements: A. B. C/D. E. F. Explain how bovine spongiform encephalopathy (BSE) occurs at a molecular level by doing the following: 1. Explain the role of prions in BSE, including each of the following: ● how prions are formed – Prions are an abnormal form of a normally harmless protein that is found in the brain and responsible for a variety of fatal neurodegenerative disease. ● the connection between misfolding and aggregation – When a protein begins misfolding it can lead to the protein aggregating, or better known as accumulating and clumping together, which can often be toxic. ● how prions lead to the disease – Prions can be found in the food in which cows eat (specifically sheep brain), when ingested, the harmful prion eventually can cause other normal proteins to begin misfolding and aggregating and than turn into harmful prions; this can take a long period of time, which leads to the build-up of these prions which eventually can lead to neurodegeneration. 2. Explain one possible role of a chaperone protein in BSE, including each of the following: ● how chaperones normally act in the cell – they assist proteins to correctly fold/assemble inside the cell ● how a chaperone protein can contribute to BSE – a defect in molecular chaperone interactions may lead to further progression of the disease instead of correction of the misfolding 3. Recommend two ways...
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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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...Task 5: Lipids A. Fatty acids come from various sources within the body. The three primary fat sources are adipose tissue (which is where fat is stored), the liver from glycolysis and fats from the food we eat. Fats are stored in the form of lipids. This covers a multitude of compounds also including hormones and other substances that tend to be hydrophobic. Triglycerides are a type of lipid composed of three bonds between a glycerol and three fatty acids (these can be saturated or unsaturated). When triglycerides are broken down they are first simplified to the singular glycerol and three independent fatty acids. The fatty acids then enter beta-oxidation where they are further broken down into acetyl-CoA which consists of two carbon and one oxygen molecule, amongst other molecules. Acetyl-CoA then enters the citric acid cycle where it generates ATP. ATP production happens during electron transport phosphorylation where NADH and FADH2 from TCA pump hydrogen protons to the intermembrane space then they follow the proton gradient back into the mitochondrial matrix through ATP synthase generating ATP from ADP B. Two key differences between saturated and unsaturated fatty acids are the chemical structure as well as shape. All fatty acids maintain four bonds to all carbon atoms. Saturated fats are “saturated” with hydrogen atoms, these tend to come from animal sources but also include cheese and the occasional plant source such as coconut. Each carbon atom has a hydrogen or...
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