Recombinant proteins containing a ________ can be purified using immobilized met
ID: 166787 • Letter: R
Question
Recombinant proteins containing a ________ can be purified using immobilized metal affinity chromatography and eluted by the addition of imidazole, a low pH buffer or a buffer containing EDTA.
Protein folding is a thermodynamically favorable process under physiological conditions because:
A) there is an increase in entropy associated with protein folding.
B) there is a decrease in entropy of the solvent by burying hydrophobic groups within the molecule.
C) of the large negative enthalpy change associated with many noncovalent interactions.
D) no intermediate stage disulphide bonds form during the folding process.
E) all of the above
Explanation / Answer
His tagged protein can be puriifed using immobilized metal affinity chromatography and eluted by the addition of imidazole, a low pH buffer or a buffer containing EDTA. 6 histidine residues are added to the N or C terminal residues of protein, this is called His tag. Histidine binds to the Ni-NTA coloum of the protein. When Imidizole is added to the Ni-NTA bed, then the bound protein is eluted as the Imidazole has high affinity with the Ni-NTA.
Protein folding is thermodynamically favorable because it spontaneously fold into native structure under normal conditions.
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