Suppose that a polypeptide contained one aspartate (Asp) residue and one arginine (Arg) residue and the polypeptide were placed in aqueous solution at a pH of 7.0. The Asp and Arg residues could be attracted to each other to form what type of intra-molecular interaction ? O London Dispersion attraction O Covalent link O Hydrogen Bonding attraction O Salt bridge O None of the above.
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A: Ionic bonds are formed between the exchange of electrons between the donor and acceptor groups.
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A: The pH of the media decides the overall charge on a molecule especially of amino acid side chains.
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Q: b the side chains of two molecules of isoleucine O ion-ion attraction O hydrogen bonding O disulfide…
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Q: Which of the groups below is capable of only hydrophobic interactions?
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A: Option A is the answer. Given,Kd = 2.55nM Kd = [A][B]/[AB] = 2.55
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A:
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A:
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- You have a mixture of 4 amino acids (Q, W, E, R, T) that you want to separate using ion exchange chromatography. Which of these amino acids would bind most strongly to a DEAE anion exchange column at pH 7? Q W E R TPolymer beads (resin) made of DEAE (diethylaminoethyl) cellulose are packed in an ion exchange column. The total mass of beads in the column is 8.47 kg. On average, each bead weighs 0.0023 g and has an average of 18.4 * 10° positively charged amine groups that can adsorba negatively charged protein that passes through the column. A solution containing 2.07 mg/L of a protein is maintained at pH 6.3 and is passed through the ion exchange column at 0.215 L/min. The protein has a molecular weight of 154,000. The pk, of the amino groups on DEAE cellulose is 7.1, and the pl of the protein is 5.6. 2. A. How long can the column be operated before reaching 80% capacity (i.e., 80% of the amino groups on DEAE are bound to the protein through an ionic bond)? You may assume that one protein attaches to one + charge on the beads (although it's possible that proteins attach to more than one + charge). B. After reaching 80% capacity, explain what you would do to release the protein attached to the…Which of the following factors do not stabilize the 3-D structure of a folded protein? O Disulfide bonds O Van der Waals interactions O Hydrogen bonds O Electrostatic interactions O Hydrophobic bonds Metal-ion protein interactions
- Indicate which of the amino acid residues in the following peptide sequence contains a group that has a positive charge for its most likely charge state at pH 10. Asp-Tyr-Lys-GIn-Thr-Ile-Phe-Met-Ser (If none of the amino acids fit the criterion, select "none".) Asp Tyr ооооооооо Lys Gln Thr lle Phe Met Ser noneA protein has an asp glu/arg lys ratio of 3. Explain how would the overall charge on this molecule likely be at pH 7 be negative?first amino acid is R second amino acid is L Draw your dipeptide at pH 7.4 What is the Log Kow of the pesticide What is the molar concentration in the octanol phase What is the number for the pesticide How many chiral centers does your assigned pesticide contain?
- The pH vs charge graph for a triprotic amino acid is shown below. Please answer the following questions about the amino acid. Net Charge 0 2 4 Alpha amino [Select] 6 R [Select] pH a. Which of the following triprotic amino acids is this? Alpha carboxyl [Select] 8 10 12 [ Select] 14 1 0.5 0 -0.5 -1 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) [Select] -1.5 c. What form of this amino acid dominates at a pH of 14? Please select the correct form for each ionizable group. -2Detergents disrupt hydrophobic interactions by coating hydrophobic molecules with molecules that have a hydrophilic surface. When hemoglobin is treated with a detergent, the four polypeptide subunits separate and become random coils*. Explain this observation.In a solution with pH ~7 most of the amino acids are form zwitterions. Name the amino acids which are charged positively and negatively and draw them in ionized forms.
- the overall, net ionic charge on this peptide at pH = 7 would be: Cys - Ala - Glu-Arg - Met - SerWhich way is more common practice to characterize the strength of a binding reaction between a protein and its ligand? Group of answer choices By its binding free energy, delta G By its equilibrium association constant K(A) By its equilibrium dissociation constant K(D) By the rate at which the biding reaction proceedsIdentify what type of chemical interactions is involved in the following side chains of the peptide chain below: 3 H-Q 0-H 5. OH OH CH, 6. 9. 4. -- CH, 2. 200 CH, 12 CH CH, -NH,0-C 4 1. 15 3. CH.-OH O CH. 17 18 The following choices can be applied for the following type of chemical interactions. 20 21 Write: AB - if it is a salt bridge or ionic bond CD - if it's a H-bonding 23 24 EF - if it's a hydrophobic interactions GH - if it's a disulfide bond