ANSWER THE FOLLOWING PROBLEM AND EXPLAIN YOUR ANSWER FOR BETTER UNDERSTANDING. 7.) Which Two Amino acids have the least solubility in water? M لهم )0 NH₂ ه
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- 1. Draw chemical structure of 20 amino acids found in the proteins (Do Not cut-and-paste images from the internet) 2. Write the full name, 3-letter, and 1-letter codes for 20 amino acids 3. Classify 20 amino acids according to the chemical characteristics Please answer very soon will give rating surely Complete Answer neededThe pH vs charge graph for a triprotic amino acid is shown below. Please answer the following questions about the amino acid. 2 1.5 1 0.5 -0.5 -1 4 8 10 12 14 pH a. Which of the following triprotic amino acids is this? Histidine b. What is the isoelectric point? (Please select the appropriate range in which the isoelectric point falls) (Hint - look up the pka values in the pKa table for amino acids, which was in video one of today's lecture) 7-8 c. What form of this amino acid dominates at a pH of 8? Please select the correct form for each jonizable group. Alpha amino NH3+ Alpha carboxyl СОО- R| NH Net ChargeDo the following a. Complete the missing bases. b. Evaluate the chain and write the polypeptide sequence. c. Identify the type of biomolecule represented by a given chain structure. Given: Biomolecule 3’ TAC_ _ _ TCT _ _ _ CCTATAGGGTCT 5’ _______________________ 5’ _ _ _ CAUAGAUUA _ _ _ UAU _ _ _ AGA 3’ _______________________ Polypeptide Sequence: ___________________________________________________________
- A protein that is normally found in an aqueous solution has these amino acids in its primary structure: glutamic acid, lysine, leucine, arginine, and tryptophan. Predict the location of each amino acid: in the interior portion of the protein (away from water) or on the outside of the protein (facing water). glutamic acid _________________________ lysine _________________________ leucine _________________________ arginine ________________________ tryptophan _________________________ Indicate whether each of the following statements describes a reversible competitive inhibitor, reversible noncompetitive inhibition, or an irreversible inhibitor. ________ a. It bonds covalently to the active site ________ b. The inhibitor effect can be reversed by the addition of more substrate ________ c. Inhibitor structure resembles that of the substrate ________ d. The inhibitor and substrate cannot bind to the enzyme simultaneously.A protein that is normally found in an aqueous solution has these amino acids in its primary structure: glutamic acid, lysine, leucine, arginine, and tryptophan. Predict the location of each amino acid: in the interior portion of the protein (away from water) or on the outside of the protein (facing water). glutamic acid _________________________ lysine _________________________ leucine _________________________ arginine ________________________ tryptophan _________________________Analyze the following biomolecule using the criteria listed below. Be sure to be clear, concise, and complete with your responses. 1. What class of biomolecules does this compound belong to? Explain why. 2. Break this compound down into its components and clearly identify each section of the molecule by labelling (circle or draw an arrow to) its backbone structure, all functional groups, and all biomolecules in the structure. 00-P-O NH3 HO
- I would like a explanation or flow of information about the Central Dogma. Include describing the structure and function of the macromolecules and four deviations of the Central Dogma. Thank you!Shown below is the structure of a polypeptide with the pK, values of its acidic hydrogens. pK = = 10.1 H OH pK, = 9.2 H. pKa = 2.1 H. N-H pK, = 6.0 pKa = 3.9 1. How many peptide bonds are present in one molecule of the polypeptide? [ Select ] II. Over what pH range would this molecule predominantly exist in a state that has a net charge of zero? [ Select ] ZIDescribe in detail why amino acids protonate and deprotonate as the pH of the solution changes. In your answer, refer to the general structure of amino acids, pKa- values, what this means and what role it plays in protonation and deprotonation of amino acids.
- Shown below are three amino acids: H,N-CH-C-o ҫн, H,N-CH-C-o CH, H,N-CH-C-o ČH, Tyrosine Tyr Y Phenylalanine Phe F Alanine Ala A 1. Which amino acid is the least hydrophobic? 2. Which amino acid is most hydrophobic? 3. Which amino acid is intermediate? 4. Explain why (2) is more hydrophobic than (3). 5. Explain why (3) is more hydrophobic than (1).Please can you answer these questions regarding the “Evaluation of the thiol content of a selection of proteins” experiment 1. Importance of protein labelling to identify constituent amino acids. Disulphide bridges 2. Why DTNB is used 3. Chemistry of reactionChoose the best answer for following question Which of the following levels of protein structure is determined byinteractions of more than one polypeptide chain?a. primary c. tertiaryb. secondary d. quaternary