...DNA and Protein Synthesis • Describe the structure of DNA and the steps of protein synthesis. The first stage is transcription, The DNA helix is untwisted by the enzyme dna helixase. Then the DNA is split into two as the hydrogen bonds are broken between the complementary base pairs, The second step is translation, which occurs in the cytoplasm and requires ribosomes. A small ribosomal subunit attaches to the bottom of the mRNA strand, and a large ribosomal subunit to the top of the mRNA. Then the synthesis can begin. For it to start the first codon (base triplet) must be methionine. Then the anticodons on a tRNA with an amino acid comes into the large ribosome unit and matches with a codon. • Describe the relationships between the following terms: o DNA- the heredity material of the cell o Chromatin material- the combination of DNA and proteins that make up the nucleus o Gene- a molecular unit of heredity of a living organism o Chromosome- an organized structure of DNA and protein found in cells • Use the following gene in protein synthesis: TAGGACCATTTTAGCCCC o Show the mRNA. o Show the tRNA. o Name the amino acids that will be placed in the polypeptide chain. (Use the codon table in Ch. 17 of Campbell Biology.) • A gene will direct the making of polypeptide chains, and polypeptide chains form proteins. All enzymes are proteins. Therefore, how would you explain carrying a gene for a trait that does not show up in the offspring? Genes can...
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...Renzo Estacio P.3 The Synthesis of a Protein Purpose: In this investigation, you will learn how to “decode” the message in this piece of DNA (the gene) and to “translate” this message into the correct protein. The central dogma of molecular biology is an explanation of the flow of genetic information within a biological system. It was first stated by Francis Crick in 1956 and re-stated in a Nature paper published in 1970. Variables: Control setup: Original DNA strand. Independent variable: The base pairing. Dependent variable: vasopressen protein Hypothesis: NONE Materials: pen or pencil, paper and lab sheet Procedures: Part A: • Make a data table and copy the letters into a section labeled DNA. • Create three more sections and label mRNA, tRNA, and amino acids. • Write down the letters that corresponds to the original DNA. Part B: • Starting from AUG in the RNA section, cirlce AUG and from there on put slashes every three letters. • Using figures 2 and 3, write down the names in three letters, below the t-RNA column, that corresponds to the t-RNA anticodons. • The proteain that should be deciphered is vasopressin. FIGURE 1 “Original DNA Sequence” A C G T A C A C G A T G A A G G T T T T A A C G G G A G C T C C T A T T A C G Figure 2: Base pairing rules for DNA with m-RNA and m-RNA to t-RNA DNA base bonds with m-RNA base bonds with t-RNA anticodes ...
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...journal entries (or the sum total, if that helps) and to synthesize some thread of thinking or learning that you find in there. You might build on a single entry or on something bridging multiple entries, but the point is to capture something that you are learning. We expect the paper to have some over-arching, coherent argument so that it is not simply a string of thoughts. A string of thoughts is fine for your journal entries, but here we do want some synthesis. You should not spend time summarizing your activities, unless that is essential for your argument. Grading Criteria The criteria we will use to evaluate the papers are listed below. Note that you do not have to address all of these criteria in one paper. We want you to address all of them over the course of the semester, but any single paper can focus on only one or two of these. Regardless of what you choose to write your reflection synthesis on, your paper must demonstrate clear, coherent argumentation. 1. Expression of Learning 2. Discussion and/or synthesis of course readings 3. Reflection on assumptions and cultural frames of reference 4. Connection to proposal process Word Count The reflection papers, except for the final one, should be at least 500 words, but not a lot longer than that. The final paper should be around 1,500...
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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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...BLUE PRINT - CHEMISTRY - Higher Secondary – Second Year Time : 3 Hours Maximum Marks : 150 S.No 1. 2. 3. 4. 5. 6. OBJECTIVES Atomic Structure Periodic Classification p-Block elements d-Block elements f-Block elements Co-ordination and Bio-coordination compounds - KNOWLEDGE E/LA SA VSA 1(3) UNDERSTANDING O E / L A SA VSA 1(1) 1(5) 1(3) 1(3) 1(1) - APPLICATION SKILL O E/LA SA VSA O TOTAL 10 09 O E/LA SA VSA 1(5) 1(3) - 1(1) - - 1(5) - - 1(5) 1(5) 1(5) - 1(1) 12 18 07 11 1(5) 1(3) - 1(3) 1(1) 1(1) 1(1) 1(1) 1(5) 1(1) - 7. 8. 9. 10. 11. 12. 13. 14. 15. 16. 17. 18. 19. 20. 21. 22. 23. Nuclear Chemistry Solid state Thermodynamics-II Chemical equilibrium-II Chemical Kinetics-II Surface Chemistry Electrochemistry-I Electrochemistry-II Isomerism in Organic Chemistry Hydroxy Derivatives Ethers Carbonyl Compounds Carboxylic Acids Organic Nitrogen Compounds Bio molecules Chemistry in Action Problems in Chemistry TOTAL 1(5) 1(5) - - 1(3) 1(3) 1(3) 1(3) 1(3) 1(3) - 1(1) 1(1) 1(5) - 1(5) 1(5) 1(5) - 1(3) - 1(1) 1(1) 1(5) - 1(5) 1(5) 1(5) 1(5) 1(3) - 1(1) 1(1) 1(1) - 1(5) - 1(5) - 1(3) 1(3) 1(3) - - 09 1(1) 09 10 1(1) 10 12 11 14 10 08 12 1(3) 1(1) 1(3) 1(3) 1(3) 2(1) 1(1) 1(5) 1(1) 1(1) 1(5) 1(5) 1(5) - 1(1) 1(5) - 1(1) 07 14 14 11 07 08 1(1) 1(5) 1(1) 1(1) - 1(1) 1(5) - 20 5 24 6 25 20 24 10 15 25 6 10 20 10 ...
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...making any substance in the body, the variability within these codes which makes who we are and different to another person is the variation of the coding of the bases (1). Task 3: The DNA stores all of the information for protein synthesis and the RNA carries out the instructions which are encoded in the DNA most of the body activities are carried out by proteins, and for the protein to be correct the sequence of the amino acid has to be therefore right. There are three kinds of RNA molecules which carry out different functions in the process of protein synthesis. One type is messenger RNA which carries the genetic information from the DNA in the form of 3 base code which the codes for an amino acid. The second is transfer RNA which is essential when deciphering the code from the mRNA so an amino acid has it won different tRNA which binds to it and takes it to the mRNA when it needs it, the correct tRNA attaches to the amino acid and is selected at each step because the Trna has 3 base sequence that can only pair with the complementary code on the mRNA. The last is ribosomal RNA which helps with the forming of the ribosomes they physically move along an Mrna molecule, they help to catalyse the amino acid into the protein chains. During protein synthesis there...
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...can be removed only by detergents that disrupt the bilayer. Peripheral membrane proteins are attatched to the cell surface electrostatically and are easily removed by altering the pH. Eucaryotic cells with outer- and intra- cellular membranes ~ half the cell’s total volume -separate intracellular organelles Nucleus- double membrane-bound organelle containing chromatin. Contains the genetic blueprint for every protein in the body. Nuclear Envelope- separates and mediates transport between the nucleus and the cytoplasm and is supported by intermediate filament proteins, the lamins. Nucleolus- dense non membrane bound structure. rRNA synthesis and ribosome assembly. Ribosome-consists of 2 subunits of ribosomal RNA. Protein synthesis- formation of peptide bonds between amino acids to make polypeptide chains using messenger RNA as a template. Endoplasmic reticulum- (rER) Protein synthesis (sER)is involved in steroid synthesis and detoxification. Golgi apparatus- determines vesicle fate. Finaly assembly and glycosylation of proteins. Mitochondria – double membrane bound energy production mainly in the form of ATP Lysosomes- high acidity, killing of pathogenic organisms, and degradation of waste products. Endosomes- Peroxisomes – production of hydrogen peroxide for killing pathogens, detoxification fo certain toxic materials, b-oxidation of long chain fatty acids, synthesis of bile acids (in liver) sole source of plasmalogens. Melanin- brown pigment in...
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...Biology Units 3 &4 Notes -Chapter 1- The Chemical Nature of Cells | |Protein |Carbohydrates |Fats |Nucleic acid | |Monomer |Amino acids |Monosaccharaide |Fatty acids, glycerol |Nucleotide | |Example |2o Amino acids |Glucose, Fructose, Ribose |Triglycerides |Adenine, Cytosine, Guanine | | | | |Steroids, Phospholipids |&Thymine/ Uracil | |Diagram | | | | | | | | | | | | | | | | | | | | | | | |Bonding (how units combine – |1st structure-strong covalent |Strong covalent glycoside |Rarely ever forms polymer |covalent bonds b/w sugar | |polymers ...
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...or more long chains of amino acid residues. Proteins perform a vast array of functions within living organisms, including catalyzing metabolic reactions, DNA replication, responding to stimuli, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific three-dimensional structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20-30 residues, are rarely considered to be proteins and are commonly called peptides, or sometimes oligopeptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residues in a protein is defined by the sequence of a gene, which is encoded in the genetic code. In general, the genetic code specifies 20 standard amino acids; however, in certain organisms the genetic code can include selenocysteine and—in certain archaea—pyrrolysine. Shortly after or even during synthesis, the residues in a protein are often chemically modified by posttranslational modification, which alters the physical and chemical properties, folding, stability, activity, and ultimately, the function of the proteins. Sometimes proteins have non-peptide groups attached, which can...
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...biological and “catalysis” means the acceleration of a chemical reaction due to a catalyst. So in general biocatalysis is the use of biological (natural) catalysts, such as enzymes. These biological catalysts are used to transform organic compounds chemically. An enzyme is a protein catalyst that is responsible for the reactions in your body. Enzymes help with digestion of food, production of essential nutrients, movement of muscles, etcetera. Enzymes not only exist in our body but are used for quite a lot of other...
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... synthesizing. E. using energy. 4. Which of the following is NOT a characteristic function of a cell? A. reproduction and inheritance B. metabolism and energy use C. movement D. synthesis E. communication 5. Which of the following could be used to study general features of cells? A. a magnifying glass B. scanning electron microscope C. transmission electron microscope D. binoculars E. light microscope 6. In order to study in detail the anatomy of internal cell parts, it would be best to use A. x-rays. B. flashlights. C. a transmission electron microscope (TEM). D. tissue cultures. E. a scanning electron microscope (SEM). 7. The plasma membrane A. separates the nucleus from the rest of the cell. B. is a rigid protein membrane. C. is not permeable. D. has a single layer of phospholipids. E. regulates movement of materials into and out of the cell. 8. The environment outside the plasma membrane is most appropriately referred to as A. intracellular. B. extracellular. C. multicellular. D. centrocellular. E. None of these choices is correct. 9. Glycolipids would contain both lipids and A. carbohydrates. B. proteins. C. electrolytes. D. cholesterol. E. amino acids. 10. The main components of the plasma membrane are A. carbohydrates and lipids. B. lipids and ions. C. proteins and carbohydrates. D....
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...Importance of DNA - A T2 Assessment Understanding what DNA is, is very important. DNA is the material that carries all the information about how a human will look (facial features, etc,.) and also how they will process daily. For example, DNA in humans determines things such as what color the eyes are, what color the hair is, and also what gender you are when a baby. DNA is found in the nucleus of almost all cells. DNA also does something called replicating nucleotides. If DNA never replicated, cell life would be impossible. If this really were to happen, the cells would then die. DNA replicates itself in order to create more DNA strands for cells. It happens along the entire DNA molecule. It continues this until the entire strand/ladder...
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...produce messenger RNA (mRNA) as well as other RNA’s. The virulent function of the mushroom acts by stopping the movement of RNA polymerase II, transcription does not occur and therefore it does not produce mRNA. The amatoxin impedes RNA polymerase at both the initiation and the elongation phase. The translation phase will not happen now due to there being no mRNA available to make proteins. Protein synthesis cannot happen, cell metabolism stops and so the cell dies. After human consumption of the mushroom, it initially can cause nausea and vomiting, but soon it affects the liver. The liver is the first organ to be damaged then the kidneys. Electrolyte imbalances begin and there would be no proteins like collagen to help with cell structure and reproduction, systems fail, and eventually, like the cell, the human dies. There is no cure. References Amanita Phalloides. (n.d.). In Wikipedia. Retrieved from http://en.wikipedia.org/w/index.php?title=Amanita_phalloides DNA Replication. (n.d.). Retrieved from http://www.tokresource.org/tok_classes/biobiobio/biomenu/dna_replication/index.htm Protein Synthesis [Internet]....
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...|Student Name |Date | | | | |Derrick Elder |9/15/2013 | |Questions |Student Response | | | | |Part I | | | | | |Original DNA Strand: |Transcription (base sequence of RNA): | | | | |3’-T A C C C T T T A G T A G C C A C T-5’ |5-A U G G G A A A U C A U C G G U G A-3’ | | ...
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...Alanine It is one of the most significant among the 20 common amino acids. It offers energy to your system. It releases into the blood stream during exercise time and induces carbohydrate-consuming effect to the health system. It promotes enhancement in the area of protein synthesis and nitrogen balance. Arginine Synthesized normally in the body, arginine is known to be a semi-essential amino acid. Sometimes more is required than normal production. Deficiencies may include poor wound healing, weakness in muscles, hair loss, irritations in skin, and constipation. Asparagine It is one of the 20 common amino acids. It is needed to maintain homeostatic balance in the nervous system. Amino acid transformation and ammonia synthesis are largely dependent on asparagine. Aspartic Acid Aspartic acid is one of two acidic amino acids belonging to the group of 20 common amino acids. It promotes enzyme activity, maintenance of solubility in the body, as well as homeostasis in ionic characters of proteins. Cysteine It is present only at the rate of 2.8% into proteins but it provides the 3-dimensional stability of the protein molecule. It also plays a crucial role in the metabolic process of many important enzymes. Glutamic Acid It is one of the important amino acid among all 20 common amino acids. It is responsible for transportation of glutamate and other amino acids to the blood barrier. Glutamine Glutamine is able to eliminate excess ammonia...
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