B
Rebesanes are made of decongribonucler
ared and proteinse
Answers
Answer:
Explanation:
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 (Figure 3.51). 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.
Figure 3.51. Amino Acid Sequence of Bovine Ribonuclease.
Figure 3.51
Amino Acid Sequence of Bovine Ribonuclease. The four disulfide bonds are shown in color. [After C. H. W. Hirs, S. Moore, and W. H. Stein, J. Biol. Chem. 235 (1960):633.]
Agents such as urea or guanidinium chloride effectively disrupt the noncovalent bonds, although the mechanism of action of these agents is not fully understood. The disulfide bonds can be cleaved reversibly by reducing them with a reagent such as β-mercaptoethanol (Figure 3.52). In the presence of a large excess of β-mercaptoethanol, a protein is produced in which the disulfides (cystines) are fully converted into sulfhydryls (cysteines).
Answer:
I think the answer is ared