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Question number 46
CORE i5 7th Gen 116 CHAPTER 4 Protein Structure 45. Laboratory techniques for randomly linking together amino acids typically generate an insoluble polypeptide, yet a naturally occurring polypeptide of the same length is usually soluble. Explain. 46. Proteins can be unfolded, or denatured, by agents that alter the balance of weak noncovalent forces that maintain the native confor- mation. How would the following agents cause a protein to denature? Be specific about the type of intermolecular forces that would be affected. a. Heat; b. pH; c. amphiphilic detergents; d. reducing agents such as 2-mercaptoethanol (HSCH CH2OH). 47. In 1957, Christian Anfinsen carried out a denaturation experiment with ribonuclease (a pancreatic enzyme that catalyzes the digestion of RNA), which consists of a single chain of 124 amino acids cross-linked by four disulfide bonds. Urea and 2-mercaptoethanol were added to a solution of ribonuclease, which caused it to unfold, or denature. The loss of tertiary structure resulted in a loss of biological activity. When the denaturing agent (urea) and the reducing agent (mercaptoethanol) were simultaneously removed, the ribonuclease spontaneously folded back up to its native conformation and regained full enzymatic activity in a process called renaturation. What is the significance of this experiment?
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