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    Understanding the Functions of Proteins and DNA Ingrid Waldron‚ Biology Department‚ University of Pennsylvania‚ 2012 These key concepts and activities are suggested as part of an introductory unit on biological molecules (or as an introduction to a unit on molecular biology). The overarching goal is to help students understand that proteins and DNA are not just abstract concepts in biology textbooks but rather crucial components of our bodies that affect familiar functions and characteristics

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    Title: Purification of Egg white protein Name: Michael Johnson Partner: David Logad & Nandita Date: 2nd – 9th September 2004 Group: Thursday 11:30am - 3:30pm Introduction Salting Out In 1888 Hofmeister that it can be possible to dehydrate a protein by adding salt to the solution‚ salting out. When a protein in a aqueous solution it is surrounded by water‚ in fact there can be up to 0.35g of water tightly bound to 1g of protein (Simpson 2004). Also the effectiveness of the salting out

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    Daniel Bergey Lab 2: Proteins and Starches Purpose The purpose of lab 2 and both tests with proteins and starches is to determine which substance contains either protein or starch. Hypothesis Proteins: I predict that any substance I test that derives from a living organism is will test positive proteins. Any substance that isn’t from a living organism more than likely will test negative for proteins. Starches: I predict that any substance that contains any level of glucose will test positive

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    Starch‚ one variable may be observed. 2. Biuret reagent will turn your skin brownish-purple. Explain why this occurs. Biuret reagent will turn your skin a brownish-purple because Iodine detects protein in a substance by changing the color to a brown or purple shade‚ and since your skin contains protein it will also change color. 3. When greasy food is spilled on clothing‚ why is it difficult to clean with water alone? Water cannot remove grease water is polar and grease is non-polar. They are

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    Experiment 2 Quantification of Proteins in Solution by Spectrophotometer Lab bench# 1 Introduction: Absorption spectroscopy is a common method for finding the concentration of proteins or protein complexes in a solution. Proteins absorb light at specific wavelengths and can be defined by the equation A = log (Io/I). This equation states that an absorbance at a specific wavelength‚ A is equal to the log of the ratio of incident light intensity (Io)‚ to transmitted light intensity (I). A

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    extra hydrogen bonds on top of each other‚ making extra-tough microfibrils that cannot be digested by most organisms. Proteins accomplish many different tasks‚ including structural support‚ storage‚ transport‚ movement‚ and defense against foreign substances. One noteworthy type of protein‚ called an enzyme‚ acts as a catalyst‚ speeding up chemical reactions in the cell. All proteins are composed of the same set of 20 amino acids‚ and each amino acid differs from the other only by the "R group" attached

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    (ELECTROPHORESIS OF SERUM PROTEIN) DATE : 10 OCTOBER 2013 PART A SEPARATION OF SERUM PROTEINS USING THE ELECTROPHORESIS METHOD. OBJECTIVES: 1. To understand the analytical methods involved in analyzing serum proteins. 2. To study the serum protein electrophoresis pattern to aid the understanding of the relationship between the structure and the function of proteins. PRINCIPLE OF PRACTICAL: This technique is based on the movement of charged particles such as proteins when placed

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    The Some of the roles proteins play in the human body like Proteins serve as enzymes‚ help maintain the body’s fluid balance by attracting water‚ help maintain acid-base balance by acting as buffers‚ act against disease agents as antibodies‚ regulate body processes as hormones‚ transport nutrients and other molecules into and out of cells‚ help clot blood‚ help make scar tissue and bones‚ and serve as light-sensitive visual pigments. Also‚ Growth and repair this the most important and Individual

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    Title: Purification of Green Fluorescent Protein Introduction: Transformation is used to introduce a gene coding for a foreign protein into bacteria. Hydrophobic Interaction Chromatography (HIC) is used to purify the foreign protein. Protein gel electrophoresis is used to check and analyze the pure protein. Research scientists use Green Fluorescent Protein (GFP) as a master or tag to learn about the biology of individual cells and multicultural organisms. This lab introduces a rapid method

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    Background: Pepsinogen is an inactive protein that is the mucus lining of the stomach. When converted to pepsin‚ the enzyme is used to break down large or undigested protein they has been absorbed by the small intestine. The digestive power of pepsin is greatest at the acidity of normal gastric juice (pH 1.5–2.5). In the intestine the gastric acids are neutralized (pH 7)‚ and pepsin is no longer effective. "Pepsin (biochemistry)." Encyclopedia Britannica Online. Encyclopedia Britannica‚ n.d. Web

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