#Question id: 880

The classic work of Christian Anfinsen in the 1950s on the enzyme ribonuclease revealed the relation between the amino acid sequence of a protein and its conformation. Ribonuclease is a single polypeptide chain consisting of 124 amino acid residues cross-linked by four disulfide bonds. Anfinsen’s plan was to destroy the three-dimensional structure of the enzyme and to then determine what conditions were required to restore the structure.

The critical observation of Anfinsen that the denatured ribonuclease, freed of urea and b -mercaptoethanol by dialysis;

I. The sulfhydryl groups of the denatured enzyme became reduced by air, and the enzyme spontaneously refolded into a catalytically active form.

II. These experiments showed that the information needed to specify the catalytically active structure of ribonuclease is contained in its amino acid sequence.

III. The 105 wrong pairings have been picturesquely termed “scrambled” ribonuclease.

IV. He found that scrambled ribonuclease spontaneously converted into fully active, native ribonuclease when trace amounts of b -mercaptoethanol were added to an aqueous solution of the protein.

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