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- Complete the table below regarding the different laboratory tests done for Amino Acids and Proteins Tests Procedure (Chemical Reagents Added) Positive Results/ Observations (ex: color of solution, precipitate formation, etc) Positive for (provide details like functional group responsible) Molisch Test Benedict’s Test Barfoed’s Test Moore’s Test Bial’s Test Seliwanoff’s Test Osazone Test Fehling’s Test Tollen’s Test Mucic Acid Test Lugol’s Test/ Iodine Test Hydrolysis w/ Benedict’s Test Hydrolysis w/ Iodine Test Provide the expected results with the samples given below: For negative results just leave it blank, for positive results write “(+) then the expected observation” ex: + blue solution Samples Molisch Test Benedict’s Test Barfoed’s Test Moore’s Test Bial’s Test Seliwanoff’s Test Glucose Galactose Fructose Ribose…Identify what test is being described: Refers to the breaking of peptide bonds that connect amino acids to compose protein ? Hydrolysis Denaturation Heat denaturation Organic solvent denaturation Biuret test Hopkins – Cole Reaction Millon’s test Ninhydrin Test Sulfur test Xanthroproteic Test Chromatography Paper chromatography Competitive inhibition Noncompetitive inhibition Rancidity Hydrogenation Identify what test is being described: Test that detects the free amino group in amino acids ? Hydrolysis Denaturation Heat denaturation Organic solvent denaturation Biuret test Hopkins – Cole Reaction Millon’s test Ninhydrin Test Sulfur test Xanthroproteic Test Chromatography Paper chromatography Competitive inhibition Noncompetitive inhibition Rancidity Hydrogenation Identify what test is being described: A foreign substance, which is structurally similar to the substrate, competes for the active site of an enzyme ? Hydrolysis Denaturation Heat denaturation Organic solvent…Give the different tests for Lipids in this tabular format:
- Ninhydrin test for amino acids or protein requires that sample test solution should be at initially basic pH. True or False?The following were obtained when testing for lipids. Discuss and conclude from the results obtained.Some characteristics of three proteins are listed in the table below: Protein Molecular Weight (Da) Isoelectric point (pI) Does the Protein Contain a heme moiety? 1 25,000 4.5 Yes 2 77,500 10.8 No 3 75,000 4.9 No a) Could gel filtration chromatography be used to separate a mixture containing Protein 1 and 2? Clearly explain why or why not. If it can be used, which protein would elute last (clearly explain why)? After collecting the fractions from the column, the absorbance of each fraction will be measured using a spectrophotometer. Can both proteins 1 and 2 be monitored at 280nm and 400nm (clearly explain)? b) Which 2 proteins listed in the table above could be separated by ion exchange chromatography but NOT by gel filtration? Why? c) Which 2 proteins listed in the table above could be separated by gel filtration chromatography but NOT by ion exchange chromatography? Why?
- Complete the table below by adding (+) or (-) if eahc sample (amino acid or protein) below will test positive or negative, respectively. sample BIURET NINHYDRIN XANTHOPROTEIC MILLON-NASSE SAKAGUCHI LEAD ACETATE PAULY HOSKIN-COLE G W H Y C R HAIR GELATIN CASEIN PEPTONE Identify the amino acid that will give the following data: BIURET NINHYDRIN XANTHOPROTEIC MILLON-NASSE SAKAGUCHI LEAD ACETATE PAULY HOPSKIN-COLE - + + + - - + - Name of amino acid: structurte of the amino acid:Sections , purine , pyrimidine sections , A,C,T,U,GSelect all that apply, meaning there can be more than one correct answer Common factors affecting menbrane fluidity include a.) Temperature. b.) presence of cholesterol c.) number of double bonds in the fatty acid chains. d.) length of phospholipid fatty acid chains Which of the following methods can seperate proteins based on their mass? a.) centrifugation b.) gel filtration chromatography c.) SDS polyacrylamide gel electrophoresis d.) ion exhange chromatography
- LABORATORY REPORT – PRECIPITATION OF PROTEINSAnalyze the image that is given below and focus on the red arrow to be able to answer the questions. Type of Bond: Choices: H-bond Electrostatic Interaction Hydrophobic bond Disulfide bond Peptide bond Level of Protein structure: Choices: Primary Secondary Tertiary Quaternary Method/s of denaturation. CHECK ALL THAT APPLY Heating to 100 degrees Celsius Addition of nitric acid Reaching Isoelectric point Addition of mercuric chloride Addition of sulphosalicylic acid Addition of alcohol Addition of ammonium sulfateWhy are we using this chemicals?(Determination of solubility and soaping number of lipids) Materials: *Fats and oils*Oil solvent (Equal volume 95% ethanol and ether)*0.5 M alcoholic KOH solution*0.05% phenolphthalein solution*0.5 M HCl solution Procedures: Determination of Saponification Number 1) Dissolve 1 g (or 2 mL) of oil in 3 mL of oil solvent and add 25 mL of KOH solution. Put a few boiling stones and boil in the water bath by mixing for 30 minutes.2) Add 3 drops of phenolphthalein to the saponified and brought to room temperature solution and titrate with HCl.3)Titrate 25 mL of KOH solution containing 2 mL of water with HCl for a blank test. Solubility of lipids 1) Record the physical properties of all oils before starting the experiment. Then observe the solubility of the oils in water and organic solvents. Discuss the difference.2) Add 1 mL of water to the oil solutions in ethyl alcohol. Mix vigorously and record your observations in the first second and after 5 minutes.