Hi can someone help me please. The picture contains the full structure.
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Hi can someone help me please. The picture contains the full structure.
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- Which reagent(s) would you use for the following processes related to protein chemistry? Write the respective equations. a) Identification of the terminal amino residue. b) Determination of the amino acid sequence of the peptide Gly-Asp-Ala-Cys c) Reversible denaturation of a protein containing disulfide bonds d) Hydrolysis of peptide bonds of aromatic residues of a protein e) Fragmentation of a protein by breaking peptide bonds on the carbonyl side of methionines.Give typing answer with explanation and conclusion On paper draw a dipeptide, clearly showing the peptide bond joining the two amino acids together. If the two amino acids are valine and threonine, predict the overall charge of the dipeptide at pH 7. Do not forget to consider the amino (N-terminal) and carboxy (C-terminal) of the dipeptide, as well as the R groups. Select one: a. +2 b. -2 c. 0 d. -1 e. +1Illustrate the asked organic compounds in the first picture. In the second picture, name the monosaccharides and their glycosidic bond.
- Explain what is meant by “The Central Dogma”? In your explanation, describe the structure and function of the macromolecules that are important in this process. Describe at least 4 deviations to the Central Dogma.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 75,000 5.0 No 2 12,500 4.8 No 3 73,000 9.8 Yes a. What type of chromatography separates proteins based on their size? b. What type of chromatography separates proteins based on their charge? c. Could gel filtration chromatography be used to separate a mixture containing Protein 2 and 3? Clearly explain why or why not. If gel filtration chromatography can be used to separate Protein 2 from Protein 3, which protein would elute first (clearly explain why)? After collecting the fractions from the column, the absorbance of each fraction will be measured using a spectrophotometer. Can both proteins (Protein 2 and Protein 3) be monitored at 280nm and 400nm (clearly explain)? d. Which 2 proteins listed in the table above could be separated by ion exchange chromatography but NOT by…Describe the mechanism behind the hydrophobic effect. Support your description with one drawing.
- A peptide was analyzed with the following results. What is the primary structure of the peptide? State what each experimental result reveals about the structure and indicate your logic. a) Amino acid analysis: R, C (2 equivalents), G, I, H, M, Y, Vb) After one round of Edman degradation, a mixture of glycine and isoleucine were detected. c) Treatment with beta-mercaptoethanol yielded two peptides, a 4-mer and a 5-mer.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?Most protein dissolve in neutral salt solution, is that true? Provide reasoning
- Discuss and identify the four levels of protein structure (primary, secondary, tertiary,and quaternary). Explain how the structure of a protein affects its properties and howdenaturation changes the structure.Using the picture provided, can you please help me with... A) which Amino Acids are Hydrogen Bond Donors? B) the 5 compouns that are most stable in the cell membrane? C) the 4 compounds that are most soluble in water? Perhaps the names of these different Amino Acids? Thank You!!The properties and biological activities of biomolecules are largely determined by their functional groups. In each of the following compounds below, circle and identify by name each functional group.