...are the proteins that cause Mad Cow Disease also known as BSE. Prions are an infectious protein. Prions are defined as an proteinaceous infectious particle, the protein is capable of changing the conformation of proteins to match its own and becomes infectious without the use of genetic materials. They can cross between species such as cattle, and sheep. Extreme heats chemical agents can inactivate the proteins. Prions are naturally occurring in the body and are not considered foreign nor do they stimulate the immune system and will not hurt your body, however the disease causing prions contact the normal prions by physical contact and alter the normal prions therefore causing the disease. With Mad Cow Disease The Prions target the specific protein in the cell that is normal called PrPC The role of protein Misfolding in BSE Diseased proteins result from improper folding and therefore the misfolded proteins induces copies of the same protein to also again misfold and increases the disease progress when it is misfolded. The scrapie prion PrPsc contacts and bumps into the normal cellular form PrPc intermediate and shifts the folding process converting them to the misfolded prion (the sheep version of mad cow disease called the PrPsc prion). The process continues over and over again. The body continues producing the normal cell PrPc and the scrapie prion PrPsc continues creating more replications of itself without needing any nucleic acid of its own. The role of protein Aggregation...
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...Protein Structure Horacio Madera Western Governors University -C624 July 2, 2015 A. Original model of the essential amino acid Threonine. B. Original diagram of the different levels of protein structure. C. Original diagram demonstrating how a peptide bond is made through dehydration. D. Original diagram that demonstrates how a peptide bond is broken through hydrolysis. E. Explanation of the four forces that stabilize a protein’s structure at the tertiary level of protein structure. Disulphide bridges are form very strong covalent bonds that are found in between Sulphur atoms in the amino acid cysteine molecules. Ionic bonds occur between a carboxyl and amino group that is not involved in a peptide bond. Hydrogen bonds result from the bonding of an electronegative oxygen atom and electropositive H atom. Hydrogen bonds can occur in either –OH or –NH groups. Hydrophobic interactions are created from certain non-polar hydrophobic amino acids that move to the center of the protein and away from the watery medium. This results in twists or folds of the polypeptide chain. Toole, G., & Toole, S. 2004, p. 38. Essential As Biology for OCR ( ed.). Cheltenham, United Kingdom : Nelson Thornes Ltd. F. Bovine spongiform encephalopathy (BSE) at a molecular level. Part F-Disease at the Molecular Level * Bovine spongiform encephalopathy (BSE) is...
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...aggregation * how prions lead to the disease A prion is a protein where the amino acid sequence or primary structure remains unchanged from that of a normal protein but the conformation has been changed by misfolding at the secondary and tertiary levels of protein structure. Bovine Spongiform Encephalopathy or BSE is a disease caused by prions. The prion which causes BSE is called PRPSC. It is the misfolded variety of the native protein PRPC. Prions are contagious. When the abnormally folded protein comes in contact with the native protein, it will cause the normally folded proteins to change their conformation to the misfolded form. The BSE prion’s changed shape or conformation causes it to be hydrophobic and therefore insoluble. The prion’s hydrophobic nature causes it to clump together or aggregate with the other hydrophobic BSE prions. These insoluble proteins aggregate or build up in the tissue and form a plaque. The plaques form on the cell membrane leading to cell death. In BSE, the cells affected are the neurons of the brain and nervous system. As the prions aggregate on the cell membrane, the neurons of the brain die leaving holes in the brain tissue that give it a sponge-like appearance. This is where the disease gets the denotation “spongiform.” As neurons continue to die off, the brain deteriorates to the point of death of the organism. 2. Explain one possible role of a chaperone protein in BSE, including each of the following: * how chaperones...
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...1.A. Original model of an essential amino acid Phenylalanine. This shows the atoms and bonds in both the backbone and the side chain. B. Original diagram of the different levels of protein structure (i.e., primary, secondary, tertiary, and quaternary). C. An original diagram, that demonstrates how a peptide bond is made through dehydration, using a complete chemical equation. Citation: Hudon-MIller, S. (2013). D. An original diagram, that demonstrates how a peptide bond is broken through hydrolysis, using a complete chemical equation. Citation: Hudon-MIller, S. (2013). E. The four forces (i.e., bonds or interactions) that stabilize a protein’s structure at the tertiary level. Hydrogen Bond this is a relatively weak bond stronger than hydrophobic bonds. Hydrogen bonds occur between one of the hydrogens on the Nitrogen molecule end of one amino acid and the oxygen molecule from the carboxylic acid end of another amino acid. The Ionic bonds are strong bonds which occur between positive and negatively charge ions of separate amino acids. Hydrophobic bonds are the weakest bonds which occur between two non-polar molecules when they come together into the interior of the structure to minimize contact with water. As the hydrophobic R groups pack together other molecules form Van der Waals...
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...Aggregates/Nuclear inclusions: Villain or tragic hero? Introduction The major defining feature of neurodegenerative diseases is the progressive accumulation of nuclear inclusions comprising of irregularly folded protein aggregates. Previously it was thought that protein aggregation is the cause of neurodegeneration as it had been established that neurodegenerative diseases such Huntington’s disease (HD), Parkinson’s disease (PD), Alzheimer’s disease (AD), prion disease, and amyotrophic lateral sclerosis (ALS) all shared a common feature which was these aggregated proteins and the formation of inclusion bodies (Ross and Poirier, 2004). However, recent studies have suggested that protein aggregation may not be the cause of toxicity to cells but that it may in fact be a protective mechanism. The aggregates formed in the above-mentioned diseases can be a consequence of mutations in the sequence of the protein that is related to the disease, increased amounts of a normal protein due to a genetic variation, or even the absence of genetic variations. These may be initiated by environmental stress or aging (Ross and Margolis, 2005). The aggregated proteins can build up and form inclusion bodies, which can be either intracellular or extracellular. There is an ongoing debate about the role of aggregation in the disease process even though one of the most common pathological features of neurodegenerative disorders is inclusion bodies. There is much evidence indicating that aggregation...
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... 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 protein and causes the protein to misfold...
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...Bovine Spongiform encephalopathy (BSE) occurs at a molecular level by infectious proteins also known as Prions. Prions can form by changes in DNA or mutations which result in a change of protein conformation. Chaperones provide an environment so proteins fold properly, bad chaperones influence the good chaperones to take form as harmful proteins. Eventually aggregates of these harmful proteins form and these aggregates lead to cell death. “The prion hypothesis suggest that diseases like BSE are caused by the misfolding of a protein known as PrP that most cells contain. Once a few copies of protein become misfolded they cause PrP’s to misfold, leading to accumulation of insoluble proteins in the cell. These misfolded proteins cause cell death and damage to the nervous system.” A country without regulations in place can help reduce risk of transmitting BSE by properly discarding possibly contaminated cattle feed. Brain and spinal cord matter should be discarded, and watching cattle with possible signs of BSE should not be introduced into the feed. One possible sign of BSE in cattle is not being able to walk, some may demonstrate aggressive behavior. The following statement is another possible way of introducing safe ways to discard contaminated cattle in a country without regulations: “According to Dr. Lisa Ferguson, a senior staff veterinarian at the Agriculture Department, said the department favored dissolving carcasses in tissue digestors, are essentially giant pressure cookers...
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...Bovine Spongiform Encephalopathy: A look at the molecular level COMPETENCY 208.5.2: AMINO ACIDS AND PEPTIDE BONDS, PROTEIN STRUCTURE BY: MELANIE MANGER Bovine Spongiform Encephalopathy Commonly know as Mad Cow Disease Although the United States has strict standards when it comes to food, BSE is absolutely an international issue A cow will ingest a food (usually a protein) that is contaminated, we as humans then in turn become infected when we eat food products made up from that particular cow Prions are an infectious agent that cause a protein in the body to fold abnormally form. Those proteins then replicate within the body and lead to brain degeneration and ultimately will cause the death of the infected individual BSE: The Molecular Level DNA makes RNA RNA makes amino acids chains of amino acids make proteins Amino acids have an amine group on one end and a carboxyl group on the other, with a Hydrogen and an R group (1 of 20 amino acids) attached to the Carbon. The amine (or amino) end of the peptide chain is known as the N-terminal, and the end with the carboxyl group is the C-terminal. Amino Acids (March 31, 2013). Retrieved July 16, 2014 from http://biochemanics.wordpress.com/2013/03/31/amino-acids/ BSE: The Molecular Level Peptide bonds are what link 2 amino acids together at the carboxyl group of one and the amine group of another Peptide bonds are created through dehydration synthesis and broken down through a process known as hydrolysis...
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...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. The PrPsc will start to influence the normal proteins and in turn cause them to take the harmful prion shapes. The PrPsc will accumulate on the cell membrane and form fibers which will cause the cell to die. Now in countries that do not have regulations in place, to decrease the risk of BSE infecting their food source...
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...Protein misfolding – hidden enemy of the brain Protein has always been a fundamental and irreplaceable biomolecule that builds up life. The studying of protein, proteomics, not only allow humans be aware of ourselves and the biosphere around us but also set the foundation for scientists to approach solutions for many human’s health problems. Among those many health issues, diseases that are associated with central nervous system raise the most concern. Many of these nervous disorders, surprisingly, are caused by the misfolding of our own human’s protein rather than any infectious virus or bacteria. Indeed, protein misfolding can bring about fatal aftermaths and consequences. One of them is very well-known deadly diseases, Creutzfeld- Jakob...
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...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 of original diagrams, that demonstrates how a peptide bond is made through dehydration. Check to see that you used a...
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...that hold a protein in its tertiary structure. Hydrophobic interactions contribute to the folding and shaping of a protein. The "R" group of the amino acid is either hydrophobic or hydrophilic. The amino acids with hydrophilic "R" groups will search for interactions with water, while amino acids with hydrophobic "R" groups will avoid water and clump towards the center protein. Hydrogen bonding in the polypeptide chain and between amino acid "R" groups helps to stabilize protein structure by holding the protein in the shape made by the hydrophobic interactions. Due to protein folding, ionic bonding can occur between the positively and negatively charged "R" groups that come in contact with one another. Folding can also result in covalent bonding between the "R" groups of cysteine amino acids, also known as a disulfide bridge (strongest bond). Van der Waals forces interactions help in the stabilization of protein structure. These interactions refer to to the attractive and repulsive forces that occur between molecules that become polarized. These forces contribute to the bonding that occurs between molecules. (Borges,2014) Bovine Spongiform Encephalopathy Mad cow disease or bovine spongiform encephalopathy is a deadly neurological disease that affects adult cattle. It is transmitted from animal to animal through contaminated food that contain infected central nervous system and spinal cord remnants. The contaminated food contain prions, a type of misfolded protein. A healthy...
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...Biochemistry Task 2 Paul A. Lebeck 000490213 January 26, 2016 A. B. (Borges, 2014, Wolfe, 2015). C. (Wolfe, 2015). D. (Wolfe, 2015). E. The forces, bonds, and interactions by protein structures at the Tertiary level. There are Hydrophobic (nonpolar), Ionic bonds, Hydrogen (covalent) bonds, and Disulfide bonds, also called Disulfide Bridges. Hydrophobic are nonpolar bonds, meaning they cannot interact with water or aqueous solutions. Hydrophobic interactions will cause the protein to change shape to avoid making contact with such solutions. Considered weak bonds, but the proteins cluster tightly together on the interior of the protein, Van der Waals interaction take place between the proteins, again these are the weakest of the molecular bonds. Ionic Bonds are by definition bonds that are made up of charged particles. There are 20 Amino Acids, some with negatively charged terminals, some with positively charged terminals. This is a basic chemistry property that opposites attract. These are considered stronger bonds, but not the strongest. Next are hydrogen bonds. Considered stronger bonds than hydrophobic bonds, but weak compared to ionic and disulfide bonds. Hydrogen bonds are formed from Polar Covalent interactions. Two amino acids share a hydrogen electron and connect on the second amino acid oxygen atom. There must be a hydrogen donor on one amino acid, and a hydrogen acceptor on a second amino acid to complete the bond. The strongest...
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... 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 that a country without regulations in place can decrease the risk of transmitting the prion involved in...
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...Protein Engineering Programme: B.Tech (Biotech) 6th Semester Course code: BIT 317 (3 credits) Unit 1 – Introduction Winter 2012-13 Dr. Everette Jacob Remington N, Ph.D Associate Professor & Ramalingaswami Fellow Biomedical Sciences Division & Gene Therapy Laboratory School of Biosciences and Technology VIT University, Vellore - 632 014, TN 1 Course objective To make the student familiarize with the basics, concepts and application of protein engineering Expected course outcome Explain the principles involved in the maintenance of protein structure Analyze the given protein structure and predict the sites to be engineered for altering/introducing a specific property 2 Course Outline Unit 1 – Introduction (9 hrs) Unit 2 – Protein Sequences and Properties (9 hrs) Unit 3 – Conformation of Proteins (9 hrs) Unit 4 – Principles and Approach (9 hrs) Unit 5 – Probing Structure for Molecular Recognition (9 hrs) 3 Unit 1 Introduction (9 hrs) Amino acid structure and properties Detection of the size of proteins Covalent structures in proteins Overview of chemical and biosynthesis of proteins Topogenesis Post-translational covalent modification of polypeptide chains 4 Amino Acids Amino acids are molecules containing an amine group, a carboxylic acid group, and a side-chain that is specific to each amino acid The amino group is attached to the carbon atom immediately adjacent to the carboxylate...
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