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    Denaturation of Proteins

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    Abstract This experiment aimed to study the effect of various denaturants on albumin and casein protein extracts through viscosity measurements. 5 mL samples of native and denatured protein solutions were prepared‚ using -mercaptoethanol‚ urea and SDS as denaturants for albumin‚ and NaOH‚ NaCL‚ HCL‚ -mercaptoethanol‚ urea and SDS for casein. 5 mL blank solutions for each denaturant used were also prepared. The viscosity of the solutions were determined using Ostwald viscometer. ________

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    Protein Denaturation

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    DENATURATION OF PROTEINS Abstract The experiment was done to be able to understand how various denaturants such as HCl and NaOH affects proteins. It was observed that different denaturants act upon or denature protein differently. This was determined using the principle of viscometry. An Ostwald viscometer was used to measure the viscosity of the prepared native‚ blank‚ denatured native and blank with denaturant solutions. The time required for the said solutions to pass through the viscometer

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    Hcl And Naoh

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    the Number of Drops of HCl and NaOH on the Net Change in the pH of Plant‚ Animal‚ and Nonbiological Solutions Research Question: How do plants and animals respond to changes in pH? Analysis Questions: Summarize the effects of HCl and NaOH on the tap water. HCl is an acid and when in tap water‚ dissociates into H+ and Cl-. Since it releases the H+ ion in the tap water‚ it raises the concentration of H+‚ which lowers the pH of the tap water. Unlike HClNaOH is a base. NaOH is a base because when in

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    Denaturation of Proteins

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    DENATURATION OF PROTEINS Abstract The experiment aimed to use the concept of viscosity to study the effects of different denaturants on 1% albumin extract. An Ostwald viscometer was used to measure the flow time of 5 mL of the blank and native protein. These were then denatured by adding 1 mL of denaturant and had their flow time measured. The flow time from the blank to denatured protein is increasing. The specific viscosity and reduced viscosity

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    Protein Denaturation

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    Practical 3: Proteins Introduction: ‘Protein’ also an important food component‚ we commonly take in from our diet. In this experiment we have studied a certain property of protein‚ i.e.‚ protein can be denatured by various factors. A. Denaturation of egg white Results: Egg white sample in water baths | Test tube | temperature | Observations | 1 | 60°C | Took 7minutes and 15 seconds to turn white and form white participate. | 2 | 80°C | Took 2minutes and 20 seconds to turn white

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    Denaturation of Proteins

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    Denaturation of ProteinsDenaturation is a process in which proteins or nucleic acids lose the tertiary structure and secondary structure which is present in their native state‚ by application of some external stress or compound such as a strong acid or base‚ a concentrated inorganic salt‚ an organic solvent (e.g.‚ alcohol or chloroform)‚ or heat. If proteins in a living cell are denatured‚ this results in disruption of cell activity and possibly cell death. Denatured proteins

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    Denaturation of Proteins

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    Denaturation of proteins involves the disruption and possible destruction of both the secondary and tertiary structures. Since denaturation reactions are not strong enough to break the peptide bonds‚ the primary structure (sequence of amino acids) remains the same after a denaturation process. Denaturation disrupts the normal alpha-helix and beta sheets in a protein and uncoils it into a random shape. Denaturation occurs because the bonding interactions responsible for the secondary structure (hydrogen

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    Formula: for NaoH N NaoH = grm KHP / ml NaoH x KHp /1000ml Formula: for HCL (NV) HCL = (NV) NaoH or N HCL V HCL = N NaOH V NaoH N HCL = VNAOH (NNaoH) / VHCL (for more info page 62-63 of the photocopy) KHP = Potassium hydrogen phthalate = KHC8H4O4 = Mw - 204.23 Trial 1: NNaoH = 1grm / 20.6 x 204.23 /1000 = 1grm / 4.21 = 0.24 normal NHCL = 20.6 (0.24) / 39.5 = 4.94 / 39.5 = 0.125 or 0.13 Trial 2: NNaoH = 1grm / 20.8 x 204.23 /1000

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    is because the protein in egg white undergoes denaturation‚ the cross linkage(the hydrogen bonds‚ ionic bonds and disulphride bonds) which maintain the protein shape destructed‚ so protein lose its tertiary conformation. This denaturing process is very important‚ because before protein can be used in digestion they must be unfolded. Part A: denaturation of egg white Aim: To examine the factors on the effect of denaturation of egg white. Principle: As protein denaturation can be cause by

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    ABABIO BUAHEN SAMUEL CHEMISTRY ONE REF. NO: 20216815 EXPERIMENT A.1.1.2 THE PREPARATION AND STANDARDIZATION OF NaOH AND HCL SOLUTION AIMS & OBJECTIVES: (1) To gain experience with titration procedure (2) To learn to standardize acid & base solution (3) To carry out the preparation of solution of a desired concentration (4) To carry out the preparation of solutions of desired concentration from more concentrated solution INTRODUCTION: Titration is a convenient quantitative method for accurately

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