|Three amino acids, alanine, arginine and aspartic acid were separated by electrophoresis at pH= 5. Indicate which amino acid belongs to the red spot, the black and blue spot, respectively. Explain your answer.
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- 10. A new protein of unknown structure has been purified. Gel filtration chromatography reveals that the physiological protein has a molecular weight of 240,000 Daltons. Chromatography in the presence of 6 M urea yields a single peak corresponding to a protein of 60,000 Daltons. Chromatography in the presence of 6 M urea and 10 mM mercaptoethanol yields peaks for proteins of 34,000 Daltons and 26,000 Daltons. What can we learn about protein's tertiary and quaternary structure from this data?6. A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography. When subjected to gel electrophoresis in the presence of SDS the protein gives three bands with molecular m of 180, 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and dithiothreitol (DTT), three bands again form, this time with molecular masses of 160, 90, and 60 kDa. a. Approximately how many amino acids are present in a 400 kDa protein. (show work) b. How many grams would there be in a nanomole of this protein? (show work) C. What is the purpose of adding DTT? d. How many subunits does the protein have, and what are their molecular weights?Consider the following properties of the protein components of a sample mixture as provided in the table below. Protein Molecular IpH Percentage of polar amino acid residues Weight (kDa) (%) АСЕ 200 7 20 CLU 25 65 DIA 100 10 40 НЕА 50 80
- 1. Suppose a protein sample with a fragment containing the following amino acid sequence is subjected to various chemical assay/tests. - Ala-Gly-Trp-Phe-Met-Cys- What is observed when the protein sample is subjected to Millon’s test? Violet interface Red precipitate/solution Brown/black precipitate Yelllow product No observable result 2. Suppose a protein sample with a fragment containing the following amino acid sequence is subjected to various chemical assay/tests. - Ala-Tyr-Trp-Phe-Cys-Gly - What is observed when the protein sample is subjected to lead sulfide test? Violet interface Red precipitate/solution Brown/black precipitate Yelllow product No observable result1. What is the name of the nucleotide shown here?2. Identify all pointed structures (A to H)3. Which structure causes the acidity of the nucleotide? Choose theletter of your answer.5. A mixture containing phenylalanine, tryptophan, and leucine was subjected to electrophoresis. Determine which of the amino acids moved the farthest distance assuming that the experiment was performed at the pH indicated: (a) pH 6.0 (b) pH 5.0
- 4. Determine the answers of these multiple choices they are organised at "a,b,c's" in which is allowed in your rules, so they can all be answered thank you very much!! A) A DNA nucleotide is composed of: *Nitrogen base *Phosphate - ribose - nitrogen base *Ribose - nitrogen base *Phosphate - deoxyribose - nitrogen base *Deoxyribose - nitrogen base B) An amino acid contains the following two groups: Acid and Thiol -Carboxyle and Amine -Carbonyl and Carboxyl -Thiol and Amine -Amine and Acid C) Which carbohydrate is part of an RNA molecule? -Ribose -Galactose -Fructose -Glucose -Deoxyriboseture.com/courses/7611/assignments/170598?module_itemid%3D695428 TR E Edulastic: Formativ. A Desmos | Testing O YouTube I Quiz | ReadTheory Quill.org - In О в, С, А, D D, B, A, C C, B, D, A How many nucleotides are represented in the diagram? * 2 points O 6 12 181. Calculate the molecular weight of protein in sample A. Given the protein migration distance is 26 mm and the migration distance of the dye front (gel length) is 6.5 cm.
- Name one purification method that can separate Protein A from a solution that contains all four proteins. (Size exclusion chromatography, ion exchange chromatography, Purification by affinity chromatography, High pressure liquid chromatography, Isoelectric focusing, SDS-PAGE, or Two-dimensional Electrophoresis) 2. In picture 3. In picture 4. In picture 5. In pictureWh 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…1. What is similar and what is different between the following chromatographic methods: Size Exclusion Chromatography; lon Exchange Chromatography; and Affinity Chromatography? This question requires you to compare, rather than simply describe the specified techniques. 2. What is similar and what is different between 1D (one-dimensional) and 2D (two-dimensional) protein gel electrophoresis? This question requires you to compare, rather than simply describe the specified techniques.