Which factor is LEAST likely to result in protein denaturation? ○ altering net charge by changing pH O changing the salt concentration ○ disruption of weak interactions by boiling O exposure to detergents ○ mixing with organic solvents such as acetone
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- What is the dissociation equilibrium constant of a protein if the concentration of free ligand is 3.0um when the fraction of bound sites is 0.6What molecule allowed our target protein to elute off our affinity column? O a. lysozyme O b. BSA O c. imidazole O d. Laemmli O e. PMSF What information can isoelectric focusing provide about a protein? choose one or more: a. its pl b. its degree of purity c. its Km d. its molecular weightWhich of the following is true regarding proteins A. Absorbance of proteins is directly proportional to the molecular weights B.Proteins react with biuret reagent because of their side chains C. two out of the twenty amino acids can absorb at 280nm D. In proteins the average weight per amino acid residue always varies
- What determines when an amino acid ionized? i.e. Why are both Lysine (pKa 10.53) and Argenine (pKa 12.48) ionized at 11 pH?A protein has a dissociation equilibrium constant equal to 4.0um. What is the concentration of free ligand when the fraction of bound sites is 0.7What would be shortest time a 250 amino acid protein would be able completely fold to the native conformation? [x] micro seconds
- Which 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 proceedsA protein-ligand binding reaction is run. At equilibrium, half the protein is ligand bound, the unboundligand concentration is 0.657 nM. Calculate the koff value for this reaction. Assume the kon value is typical ofprotein-ligand interactions.When a protein is denatured using heat Select one: a. its C-terminal will change. b. its tertiary structure will change. c. its amino acid sequence will change. d. its amino acid composition will change.
- What happens when the temperature of a protein is lowered below its optimal temperature chose all that applyWhat is the difference between the two salt precipitation methods: salting in and salting out? Group of answer choices Salting in relies on the isoelectric pH of the specific amino acid residue whereas salting out relies on the charge of the specific amino acid residue. Salting in relies on the charge of the specific amino acid residue whereas salting out relies on the isoelectric pH of the specific amino acid residue. Salting in decreases salt concentration thereby increasing the solubility of the protein whereas salting out increases the salt concentration to precipitate out the protein component. Salting in increases salt concentration thereby increasing the solubility of the protein whereas salting out decreases the salt concentration to precipitate out the protein component.A new amino acid is found with the alpha N and backbone COOH pKa's the same as histidine but with a neutral side chain. What is the isoelectric point of this new amino acid?