Q. Proteins and macromolecular structures take on their higher order structures

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Q. During successful purification scheme, this may be expected that the

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Q. In ion-exchange chromatography

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Q. Which of the following may be added to stabilize the protein after yeast cells disruption?

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Q. Gel-filtration chromatography separates on the basis of

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Q. Affinity chromatography deals with the

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Q. A purified protein sample contains 10 μg of protein and has an enzyme activity of 1 m mole of ATP synthesized/sec (1 unit). What is the specific activity of the final purified sample?

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Q. Proteins separation can be carried out on the basis of

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Q. The best way to determine the location of protein in the purification scheme is to measure the

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Q. The conformational changes from the T to the R state is initiated by

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Q. An allosteric activator

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Q. Bisphosphoglycerate (BPG) cannot bind to the oxygenated R state of hemoglobin because

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Q. The Hill coefficient (nH) for myoglobin and hemoglobin are respectively

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Q. When protein binds two ligands in a non-cooperative manner, then the x-intercept of the Scatchard Plot is

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Q. O₂ binding to hemoglobin results in

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Q. In hemoglobin, allosteric effects occur

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Q. A protein that binds two ligands in a non-cooperative manner will show

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Q. Small molecules affect hemoglobin (Hb) by

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Q. A protein that shows infinite cooperative for binding of n ligands will

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Q. The specificity of a ligand binding site on a protein is based on

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