Acids‚ Bases and Buffers Lab Acids‚ Bases and Buffers Lab Results: The experimental results for part one is as follows: Part One Data Table | Initial pH | Final pH | Test Tube A | 6 | 1 | Test Tube B | 4 | 4 | Test Tube C | 4 | ----- | Test Tube D | 4 | 4 | Test Tube E | 6 | 11 | The experimental results for part two is as follows: Part Two Data Table | Before CO2 was Added | After CO2 was Added | Colour | Blue/green | Light green/yellow | pH Level | 8.0pH | 5.0pH |
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non-essential amino acids‚ amino acid remodeling‚ and conversion of non-amino acid carbon skeletons into amino acids and other derivatives that contain nitrogen. However‚ the liver is the major site of nitrogen metabolism in the body. In times of dietary surplus‚ the potentially toxic nitrogen of amino acids is eliminated via transaminations‚ deamination‚ and urea formation; the carbon skeletons are generally conserved as carbohydrate‚ via gluconeogenesis‚ or as fatty acid via fatty acid synthesis pathways
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DKFLSDFKLFKJ | Acid-Base Titration. | kfjhdkjhvdkfj | | April Jowers | 12/19/2012 | DKFJSDKJFHDSKJHF | Introduction In this lab we will use basic titrating skills and techniques in order to titrate HCl. We will also be practicing how to prepare the solution. Using the titration data‚ we can practice our stoichiometric skills and also become more familiar with using lab equipment. Titration is the process of measuring the exact volume of a solution of known concentration that is
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Determination of Unknown Acid KEYWORDS: quantitative analysis‚ titration‚ buret‚ endpoint‚ standardization‚ half-equivalence point‚ calorimetric titration‚ potentiometric titration ABSTRACT: The concentration of sodium hydroxide was determined by colorimetric titration‚ and the identity of an unknown acid was determined by potentiometric titration. In the first titration‚ a strong acid standard‚ potassium hydrogen phthalate (KHP)‚ was used‚ to determine the concentration of a strong base‚ sodium hydroxide
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The charts below lists a portion of the amino acids found in the Cytochrome C protein of several different organisms. Use the chart to compare the amino acid sequence in humans to the sequences of the other organisms listed. For each organism‚ identify any amino acid that is different or missing when compared to the amino acids in the human sequence. 1. 2. 3. 4. 5. 6. 7. 8. Click on the following link to open the activity chart: Amino Acid Sequences in CytochomeC Proteins.
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Result: Part A: Table 1: Fractionation of amino acid Fraction No | Response to Ninhydrin test(level of blue colour change) | Response to Sakaguchi test (colour change) | 1 | X | yellow | 2 | Dark blue | yellow | 3 | Dark blue | Pale orange | 4 | Blue | Pale orange | 5 | Pale blue | Pale orange | 6 | Blue | Pale orange | 7 | Pale blue | Pale orange | Discussion Part A In the separation and purification of a single protein or amino acids‚ a solution containing the desired analyte
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Benedict College Acid- Base Titration Jorge Moreno Chem 118LS4-133S Mr. Qin Purpose In the lab they want determine the concentration of a solution. One way that they have to
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Acid/ Base Titration Lab Design III Materials: Goggles HCl NaOH Distilled Water Label Beaker Graduated Cylinder Pipet Stirring rod Buret with clamp Stopper Ring Stand Utility Clamp Computer Computer Program pH probe Procedure: 1) 2) Goggles were put on. 3) 0.1 M NaOH solution was made using 0.4 g NaOH and 100 mL distilled water. The ingredients were added together in a beaker and stirred. 4) The buret was standardized by adding 10 mL of distilled water‚ rolling
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Electrophoresis of Amino Acids Introduction: Electrophoresis is a separation technique based on the movement of charged ions under the influence of an electrical field. This technique is primarily used for the separation of amino acids and peptides on the basis of their charge. All amino acids contain ionizable groups that cause the amino acids‚ in solution‚ to act as charged polyelectrolytes that can migrate in an electric field. The amino acids with a net positive charge will migrate toward
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Alanine (ala‚ A) (neutral‚ non-polar) Arginine (arg‚ R) (basic‚ polar) Asparagine (asn‚ N) (neutral‚ polar) Aspartic Acid (asp‚ D) (acidic‚ polar) Cysteine (cys‚ C) (neutral‚ slightly polar) Glutamic Acid (glu‚ E) (acidic‚ polar) Glutamine (gln‚ Q) (neutral‚ polar) Glycine (gly‚ G) (neutral‚ non-polar) Histidine (his‚ H) (basic‚ polar) Isoleucine (ile‚ I) (neutral‚ non-polar) Leucine (leu‚ L) (neutral‚ non-polar) Lysine (lys‚ K) (basic‚ polar) Methionine (met‚
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