Which of the following of immunoglobulin inflexible:
- a. IgG
- b. Ig M
- c. Ig A
- d. Ig D
- e. IgE***
The correct answer is e. IgE.
The correct answer is e. IgE. Immunoglobulin E (IgE) is the most flexible immunoglobulin among the five classes of immunoglobulins. This is due to its unique hinge region, which is composed of fewer amino acids compared to the hinge regions of other immunoglobulins. The reduced number of amino acids in the hinge region of IgE allows for greater flexibility, enabling it to better adapt to different conformations upon binding to allergens.
Here's a summary of the flexibility of each immunoglobulin class:
- IgG:
IgG is the least flexible immunoglobulin due to its long hinge region, which contains numerous disulfide bonds that provide rigidity. The reduced flexibility of IgG contributes to its stability and persistence in circulation.
- IgM:
IgM has a slightly more flexible hinge region than IgG, allowing for some degree of conformational adaptation. This flexibility is thought to contribute to IgM's role in complement activation.
- IgA:
IgA has a hinge region of intermediate flexibility, allowing for moderate conformational changes. This flexibility is thought to be important for IgA's function at mucosal surfaces.
- IgD:
IgD has a hinge region similar in flexibility to IgA, enabling moderate conformational adaptation. The exact function of IgD's hinge region is not fully understood, but it may play a role in B cell activation and maturation.
- IgE:
IgE has the most flexible hinge region among all immunoglobulins, allowing for significant conformational changes. This high flexibility is crucial for IgE's ability to crosslink mast cells and basophils, triggering allergic reactions.
Therefore, IgE is the most flexible immunoglobulin due to its unique hinge region structure, which contributes to its ability to bind allergens and trigger allergic responses.
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