Questions Nguy sapreds Tagab Fitn nass 1. An unknown protein yielded the following test results using the procedure in this experiment. Based on these results, what amino acids must be present in the protein? Sp د مرور test ninhydrin xanthoproteic Millon's Hopkins-Cole nitroprusside observation yellow observation (+) yellow solution (+) red precipitate (-) colorless (+) purple solution o di tin E to mi LA HOR
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- SDS-PAGE gels are useful in determining the molecular weights of proteins; however, the molecular weights of are usually not reliable. proteiI. A protein, X, was Isolated from a pathogenlc mlcroorganism. The proteln Is a vlrulence factor whose path0genlclty lies In a heptapeptide of unknown sequence. After trypsin cleavage of the heptapeptide from protein X, the peptlde's compOsition and sequence was determined. The fOllowing were the results of the sequenclng process: 1. When the peptide was treated with dinitrofluorobenzene (DNFB), DNP-asp and a mixture of amino acids were produced. 2. When the same Intact peptide was treated with streptococcal protease, a pentapeptide of composition asp, asN, cys, gly and ser and 2 amlno acids were released. 3. When the heptapeptlde was also treated with hydrOxylamine HCI, a tripeptide and a tetrapeptide were obtained. The C-terminal amino acid of the tripeptide was asN. 1) What is the sequence of the heptapeptide if it is composed of cys, asp, lys, asN, gly and ser only? 2) What is the pl of the heptapeptide?Wh are doing this procedures can you explain? (ex. heating or adding chemicals etc.) 1) Purification of Vitelline from Egg Yolk-Experimental ProcedureMeasure the volume of 3 egg yolks and mix by adding an equal volume of NaCl solution.Extract the mixture with 3-fold volumes of ether and separate the aqueous phase.Do the same procedure 3 times.Mix the sample with water and rinse.It is expected for the protein to collapse.Some more water is added in order to check whether the collapse occurs completely.The sample is centrifuged and the precipitate is dried. 2) Purification of Plasma Albumin and Fibrinogen-Experimental ProcedureAdd ammonium sulfate to 10 ml plasma up to 25% saturation.Separate the collapsed fibrinogen by centrifuge.Increase the saturation level to 33% by adding (NH4) 2SO4.Separate the globulin by centrifugation.Separate prodoglobulins by increasing the saturation level to 46%.Increase the saturation level up to 64% to precipitate albumin.Separate the albumin by centrifuge…
- Electrophoresis A protein required 6.8 min to travel 82 cm to the detector in a 96 cm -long capillary tube with 25.4 kV between the ends. Find the apparent electrophoretic mobility.What can be the interpretation for the results given below? Test/s Results Ninhydrin Xanthroproteic Millon's + Biuret Pauly O The unknown sample contains tyrosine and tryptophan residues O The unknown sample only contains tyrosine as free amino acids The unknown sample contains tyrosine and histidine residues O The unknown sample contains tyrosine, tryptophan, and histidine residuesExplain the advantage of using Fluorescence Recovery After Photobleaching (FRAP) in determining protein localisation I notes = Notes Comments MAY 7.
- PROTEINS 1. What will happen to free arginine after being subjected to biuret analysis (is it positive or negative, include color)2. What will happen to beef extract after being subjected to ninhydrin analysis (is it positive or negative, include color)Example of a Protein Purification Scheme: Purification of the Enzyme Xanthine Dehydrogenase from a Fungus Volume Total Total Specific Percent Fraction (mL) Protein (mg) Activity Activity Recovery 1. Crude extract 2. Salt precipitate 3. Ion-exchange chromatography |4. Molecular-sieve chromatography 5. Immunoaffinity chromatography 3,800 22,800 2,460 0.108 100 165 2,800 1,190 0.425 48 65 100 720 7.2 29 40 14.5 23 1.8 275 152.108 11 Calculate the specific activity of step#4. Note that percent recovery=% Yield.What's the amount of protein if the measurement at A280 = 1.120, dilution factor is 100 and total volume of extract is 45
- a. State the importance of using following reagents in SDS-PAGE. 1. Acrylamide 2. Bisacrylamide 3. Tetramethylethylelediamine 4. Glycerol 5. Ammonium persulfate b. Briefly describe the importance of two dimensional electrophoresis in protein separation?topic: Bradford AssayThere are numerous methods of protein determination in use, but this module focuses on the Bradford assay.The Bradford assay is a dye-binding method that employs Coomassie Brilliant Blue G-250, whose structureis shown in Figure 2.3.4.1. Coomassie Brilliant Blue G-250 is a dye that interacts with proteins throughhydrophobic and electrostatic interactions. What are the identities and functions of the components of the Bradford reagent in protein contentdetermination?E Classwork for BTMF_Itani_ Biolo X E SI'ERRA STANLEY - protein-synth X arch 8 period light reaction - Google S x ocs.google.com/document/d/1plhyciPrM-AMsQKmaUHZSZU44EJL85jDuCyDxE01E60/edit LEY-protein-synthesis-worksheet_practice-converted ☺ Insert Format Tools Add-ons Help Last edit was 5 minutes ago 100% Normal text Noto Sans . BIUA 12 川, 三= + - I 1. 2 . 4. 5 PART C. Use your codon chart to determine the amino acid sequence. Remember to read through the strand and ONLY start on AUG and STOP when it tells you to stop. Follow example below: Example: DNA O AGA CGG TAC CTC CGG TGG GTG CTT GTC TGT ATC CTT CTC AGT ATC mRNA O UCU GCC AUG GAG GCC ACC CÁC GAA CAG ACA UAG GAA GAG UCA UAG protein 0 start - glu – ala -thre - hist – asp -glu-threo-stop acid acid 1. DNA → CCT CTT TAC ACA CGG AGG GTA CGC TAT TCT ATG ATT ACA CGG TTG CGA TCC ATA ATC MRNA → protein → 2. DNA → AGA ACA TAA TAC CTC TTA ACA CTC TAA AGA CCA GCA CTC CGA TGA ACT GGA GCA MRNA → protein → 围 Sign out Co & 6. 7