2. Explain the following situations: a. Why do antibodies to antibodies raised a

Question

2. Explain the following situations: a. Why do antibodies to antibodies raised against a particular enzyme occasionally bind the enzymes substrate with a high degree of specificity? b. Why do antibodies raised against a transition-state analogue of a particular reaction occasionally catalyze the reaction? e. Why do antibodies raised against a native protein rarely bind to the denatured form of the protein? HINT: In class we have discussed certain molecules binding to G-protein coupled receptors or other targets (epinephrine binding to its receptor for example). In its simplest form, this form of binding can be described in the same way as a substrate binding to an enzyme. When answering this question, think in terms of enzyme binding and review the section on weak enzymatic interactions (pg. 189-191).

Explanation / Answer

a.

Antibody molecules are large proteins. Antibody detect the diseases biomarkers. Antibody to antibody interactions has high degree of specificity because they have structural similarities.

b.

Enzyme-substrate complex is the transition state. In this state also enzyme-substrate complex also have same structural similarity with antibody. So that antibody raised against a transtion state.

c.

Denaturation destroy the structure of the enzyme. So that the structure of protein for binding antibody will change. Therefore, antibody rarely raised against to bind the denaturad form of protein.

Related Questions

Navigate

• Browse (All)
• Browse 2
• Subjects

---

---

Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.