...What is Biochemistry and why you should study it? Biochemistry or sometimes we called it as biological chemistry is defined as a scientific study of the chemistry of living organisms, especially the structure, the behavior of a living thing and the function of their chemical component such as proteins ,carbohydrates, lipids, and nucleic acids. Many of these molecules are complex molecules called polymers, which are made up of monomer subunits. Most people consider biochemistry to be same with molecular biology. Nowadays, biochemistry has become the root for understanding all biological processes. It has provided widely explanations for the causes of many diseases in humans, animals and plants. As a student, we should study it because it give to us many kind of knowledge on understanding the biological processes which are happen around us in every single minutes in our life. Since biochemistry is very important, we must study it to know how this biochemistry contributed for the sustainable of tomorrow in the main field of medicine, agriculture and industry. Biochemistry is applied in many health field such as dentistry, medicine and veterinary medicine. For example, in the field of medicine, biochemistry have contribute in the clinical study to maintain and to give a better and healthy life to the population of human all around the world. This have been done by the scientist on how they use biochemistry to diagnose and control the spreading of diseases, product a new...
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...Date Sheet for Sciences General/ Core Courses/All Major Mid Term Examinations -Fall 2013 Semester Date & Day Sem 09:30 -11:00 Sec No. Room No. Teacher's Name Tooba Mohtsham Dr. Shahnaz Ch. Dr. Shahnaz Ch. Sem 11:30 -01:00 Sec No. Room No. Teacher's Name Sem Asifa Kayani Dr. Nikhat Khan 7 7 7 01:30 -03:00 Sec No. Room No. Teacher's Name 1 Introductory Biochemistry Introduction to Biotechnology Molecular Biotechnology A A A 9 35 4 Sci Y Sci Y Sci Y 3 3 Microbiology Electricity and Magnetism A A 56 31 NB-15 NB-8 Data Analysis & Report Writing A Data Analysis & Report Writing B Data Analysis & Report Writing C 33 NB-14 Farah Arif Munaza Bajwa Itrat Batool Naqvi 21-Oct-13 1 5 41 Main Lab NB-7 1 1 English-I English-I N K 25 44 SCI Y SCI Z Sadia Ghaznavi Nasreen Pashsa 3 Mathematics A 28 NB-36 Nighat Altaf 5 Molecular Physiology A 16 SCI 9 SCI 6 SCI 8 SCI 12 SCI 12 Tooba Mohtsham Asifa Kayani Saleha Mehboob Ayesha Aftab Gaitee Joshua 22-Oct-13 Basic Concepts of Environmental Sciences 24 5 A Data Handling and Atomic Spectroscopy 5 A 5 5 Electrical Instrumentation Human and Animal Behavior A A 9 9 12 7 Advanced Topics in Molecular BiologyA 7 7 Medical Biotechnology Plant Ecology A A 19 33 3 SCI 6 SCI R SCI 6 SCI 7 SCI 7 SCI 8 SCI8 Dr.Hooria Younas Dr. Amber Shehzadi Asifa Kayani Ayesha Roohi Saleha Mehboob Saima Mubeen Dr. Saleema...
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...Biochemistry Empirical procedure for purifying Enzyme X: 1. To begin the purification process, mix blue green algae with an appropriate quantity of a buffer and triturate through use of a mechanical crushing process. Centrifuge at 4 degrees C for 10 min at 5,000 rpm. Next, determine whether the supernatant and the precipitate has the highest specific activity of the desired enzyme. The specific activity is the ratio of biochemical activity to the weight or volume of total protein present. The portion containing the greatest concentration of the desired enzyme would be kept for further fractionation and testing. Use of substances such as ammonium sulfate or polyethylene glycol that compete for water with the macromolecules could then be employed. This process, known as "salting out" the organic material from water by varying the solvent ratio or through doing another assay measuring the specific activity. Again, the portion containing the lesser amount would be discarded. Affinity chromatography would next be performed to identify the active enzyme based on the principal that enzymes attach to specific substrates and that specific receptors selectively bind the enzyme, impeding its passage in solution. Next, electrophoresis would be performed to help determine the purity of the compound. In electrophoresis, substances are first sorted by size and charge, and then by charge. There will be a separation of bands in the electrophoresis that corresponds to the...
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...Biochemistry Task 1 Sandra Clem 000448176 September 7, 2015 A. ( https://bnzm.files.wordpress.com/2010/09/dnareplication.jpg ) B. ( https://bnzm.files.wordpress.com/2010/09/dnareplication.jpg ) C. ( http://limbiclab.files.wordpress.com/2012/12/limbic_lab_levinandtijan2003transcriptionreg ulationandanimaldiversity.pdf ) D. The toxins that the death cap mushroom produce work against the enzyme RNA polymerase by stopping the transcription process. This in turn causes a domino effect as the mRNA will be stopped and no proteins will be regenerated from the cell. All of our tissues need protein to survive. If the death cap mushroom is ingested it starts this process in the GI tract. The liver and kidneys are filters for toxins and they try to filter the toxins. These toxins are prohibiting tissue repair by blocking RNA polymerase and no proteins can be made from mRNA this process causes liver and kidney failure and can cause death if not diagnosed early on. ( International Journal of Hepatology Volume 2012, http://dx.doi.org/10.1155/2012/487480) E. eferences R HudonMiller, S. (2012) Death cap mushrooms. Retrieved from https://wgu.hosted.panopto.com/Panopto/Pages/Viewer/Default.aspx?id=45c5aef2370e43ebad 9c40f073926331 . International Journal of Hepatology (Volume 2012), http://dx.doi.org/10.1155/2012/487480 ...
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...Isolation of Alkaline Phosphatase from E. coli Josh Brooks Department of Chemistry and Biochemistry, McMurry University, Abilene TX 79697 Abstract: In this experiment our goal was to analyze alkaline phosphatase from E. coli .In order to do this the purification of a protein from E. coli many steps were done through multiple weeks of assays. Finally, once the desired protein was pure a Bradford and a gel can be run to be sure that the protein was indeed purified. Introduction: In order to purify the protein many step are needed and the analyte should be evaluated by measuring the concentration and the activity of the protein. Physical and biological properties are used to help determine purity. These factors can be used to distinguish the analyte from other proteins. Located in the periplasmic space, the space between the cytoplasmic member and the outer membrane, alkaline phosphatase is cleaved and provides the cell with inorganic phosphate. To get a large enough sample of alkaline phosphatase the K12 mutant of E. coli is used. This mutant is unregulated in the cell because it lacks a way to control alkaline phosphatase production. Alkaline phosphatase is best used in acidic conditions and is very stable at high temperatures. By taking advantage of these two properties alkaline phosphatase can be isolated from the other proteins in E. coli. The overall goal is to reduce the total amount of protein but increase the specific activity of the desired protein. The experiment...
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...should have an idea on what school you would want to attend. Most doctors would say that they have a list of 3 or 4 schools that they would attend. They would contact the schools and see what is required for undergrad work. So I decided to check out NECO (New England College of Optometry) I chose NECO because it is one of the top schools in the country and it is based out of Boston too. Applicants to the Doctor of Optometry program need to demonstrate at least three years of undergraduate preparation. Within this period of study the student must have credits for the following specific course work: (NECO 2015) Biology with Lab 2 Semesters Chemistry with Lab 2 Semesters Physics With lab 2 Semesters Organic Chemistry with lab 1 Semester Biochemistry 1 Semester Microbiology 1 Semester Calculus 1 Semester Statistics 1 Semester Psychology 1 Semester English 2 Semesters Looking at this, You can get your English...
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...Carbohydrates Carbohydrates are the sugars, starches and fibers found in fruits, grains, vegetables and milk products. They are called carbohydrates because, at the chemical level, they contain carbon, hydrogen and oxygen. Carbohydrates provide fuel for the central nervous system and energy for working muscles. Carbohydrates are classified as simple or complex. Simple carbohydrates contain just one or two sugars, such as fructose (fruits) and galactose (milk products). These single sugars are called monosaccharides. Carbs with two sugars — such as sucrose (table sugar), lactose (dairy) and maltose are called disaccharides. Complex carbohydrates, which are also called polysaccharides have three or more sugars. They are often referred to as starchy foods and include beans, lentils, potatoes, corn, whole-grain breads and cereals. Lipids Lipids are molecules that contain hydrocarbons and make up the building blocks of the structure and function of living cells. Examples of lipids include fats, oils, waxes, certain vitamins, hormones and most of the non-protein membrane of cells. Lipids are not soluble in water. They are non-polar and hydrophobic. Lipids contains a functional group including neutral fats, waxes, phospholipids, and glycolipids. The fatty acids with no carbon-carbon double bonds are called saturated. The ones that have two or more double bonds are called polyunsaturated. Proteins Proteins are large biomolecules, or macromolecules. They are made up of hundreds or...
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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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...Smith 1 Heather Smith 477126 Biochemistry WGU August 24, 2015 Smith 2 Model of Essential Amino Acid Essential amino acids are those amino acids in which the body can not make on its own, instead they must be procured through the foods that we eat (Helmenstein). Lysine is one of the essential amino acids. Two of the chemical properties of lysine are that it is positively charged and it is hydrophilic, which means water loving so it easily dissolves in water (National Center for Biotechnology Information). Smith 3 Each NH2 contains one nitrogen atom and two hydrogen atoms represented on the diagram as intertwining pipe cleaners color coded to there respective elements (ie NH2 has blue and neon) Each CH2 contains one carbon atom and two hydrogen atoms (pink and neon) OH contains one oxygen atom and one hydrogen atom (orange and neon) Diagram of Protein Structure Smith 4 Dehydration : Creating a Peptide Bond Smith 5 Diagram: Peptide Bond Broken by Hydrolysis Smith 6 The Four Forces that Stabilize Proteins at Tertiary Level The tertiary structure of proteins are dictated by several factors. Non polar molecules are also hydroph...
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...There are several differences between unsaturated and saturated fatty acids. Unsaturated fatty acid is made of carbon and hydrogen bonds that does not mix well with water. Unsaturated fatty acids are solids at room temperature. They are found in food sources such as cheese, red meats, coconut oil, whole milk dairy products. Unsaturated fatty acids are structurally designed with a single carbon of a single carbon double bond, and hydrogen bonds. They are liquids at room temperature. Unsaturated fatty acids include food sources such as plant based oils, flaxseeds, walnuts, salmon, and unhydrogenated soybean oil (Sanders, 2013). The body is able to use fats for energy storage and metabolism of adenosine triphosphate (ATP). Adipose tissue stores fat. Triglyceride is a fat storing molecule. Fatty acids and glycerol are components of triglycerides. Fatty acids are separated into two carbon units, which produce acetyl coenzyme A (acetyl –CoA) during the process of beta oxidation. Electrons and hydrogens are extracted from the fatty acid. Nicotinamide adenine dinucleotide (NADH) and flavin adenine dinucleotide (FADH2) are created and transferred to electron transport chain for creation of ATP. Acetyl-CoA enters the citric acid cycle via beta oxidation pathway. The electrons and hydrogens are expelled and moved to electron transport chain for production of ATP (O’Malley, 2014). A deficiency of linoleic acid (LA) will affect the biochemical functions of the body. Linoleic acid...
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...There are four macromolecules that make up all living things. These macromolecules are proteins, carbohydrates, lipids, and nucleic acids. All of these macromolecules are formed from functional groups. The functional group hydroxyl is found in every macromolecule. All of these macromolecules except for lipids are hydrophilic. All of these macromolecules are broken down into monomers by hydrolysis reactions. Proteins have methyl groups, amino groups, and carboxyl groups. Proteins are polymers of amino acids. Proteins functions are determined by how they are folded. Proteins with a primary structure have no function. Proteins with a secondary structure are in the shape of an alpha helix but still have no function. Once a protein achieves tertiary structure that protein has a function. Quaternary structures in proteins are made of many motifs and have the most advanced functions of all the structures, many of them being enzymes due to their three dimensional structure. However, a protein can become unfolded, and once it does it cannot be reversed, this is called denaturation and makes the protein loose its functions. All proteins and polypeptides are links of amino acids held together by peptide bonds. Peptide bonds are formed between two molecules when the carboxyl group and the amino groups in two atoms react which causes dehydration synthesis. Carbohydrates have carbonyl groups, and are organic compounds every time due to the presence of a carbon atom and also have hydrocarbons...
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...Introduction: Yeast cells are simple, unicellular, eucaryotic organisms belonging to the Fungi kingdom. These cells are particularly important as tools for research because they share structural and compositional similarity with cells of higher organisms. This experiment makes use of these similarities to study individual macromolecular components found within all living cells. Through this experiment we will learn the basic sub-units that make up each of these macromolecules while also learning some of their important structural characteristics. This experiment will consist of two parts. The first of which will divide the yeast cells into three of its major macromolecular components: nucleic acids, proteins and polysaccharides. These components are large macromolecules that are quite unique in their composition, structure and function. However, they share a common feature as each macromolecule is composed of repeating subunits, characteristic of the macromolecule. The subunits are linked together by a bond between two adjacent subunits, formed by the loss of water (condensation). Thus, macromolecules can be broken down by the addition of water across the bond, in a process known as hydrolysis. This process was used in the experimental procedure to allow analysis of each individual macromolecule in its subunit form. Proteins are hydrolyzed into amino acids, nucleic acids are hydrolyzed into sugar, base and phosphate, and polysaccharides are broken down into simple sugars...
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...Biochemistry Task 3 A. (HudonMiller, Hemoglobin…, 2012) 1. Two differences between oxygenated and deoxygenated hemoglobin are shape and color. Color change is reflected in the amount of oxygen bound to the hemoglobin. The more oxygen there is, the brighter red the hemoglobin will be. In the oxygenated state the shape changes as well. In this state, the protein is in what is known as the R or relaxed state. (HudonMiller, 2012) When the oxygen leaves the the hemoglobin the heme changes to a dome shape, which in turn, changes the shape of the protein. This is known as the T or tense state. (HudonMiller, Oxygenated....,2012) 2. Oxygen binds more at higher pH and is released better at a lower pH. Our lunges are higher pH which is where hemoglobin gets saturated with oxygen. Our periphery is more acidic at a lower pH. Hemoglobin is able to release oxygen easier at lower pH levels. This is what allows oxygen to make it to our fingers and toes. (HudonMiller, The Bohr…,2012) 2a. (HudonMiller, The Bohr…,2012) 3. (HudonMiller, Hemoglobin vs…,2012) B 1. ...
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...DNA Replication Jennifer Wilson Biochemistry GRT1 Margie Hayes January 18,2015 Deoxyribonucleic Acid (DNA) DNA is made of chemical building blocks called nucleotides. These building blocks (nucleotides) are made of phosphate, sugar and one of four types of nitrogen bases. The four types of nitrogen bases found in nucleotides are: adenine, thymine, guanine and cytosine. These nucleotides are either purine or pyrimidine based, called nucleotide subunits. The purine base are adenine and guanine. The pyrimidine based are thymine and cytosine. The DNA strand is formed when the nucleotides are linked into chains, with the phosphate and sugar group alternating. As you can see in the diagram above, adenine bonds with thymine and guanine bonds with cytosine. These bonds take place by hydrogen bonding. DNA Replication Fork Topoisomerases are enzymes that regulate the overwinding or underwinding of DNA, shown as the yellow wire above. Topoisomerases catalyze and guide the unknotting and unkinking of DNA. The double-helical configuration that DNA strands naturally reside makes them difficult to separate, so they must be separated by helicase enzymes. Helicase separates the strands of a DNA double helix by using the energy from ATP hydrolysis so replication can begin. The replication bubble allows replication to take place in 2 directions. Primase is an enzyme that synthesizes short RNA sequences called primers. These primers are the starting point for DNA synthesis at...
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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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