Each immunoglobulin (Ig) domain is composed of a structure known as a '$\beta$-sandwich,' which consists of two $\beta$ sheets covalently linked by a disulfide bond. Only a subset of the ~110 amino acids in each domain are required to establish this overall structure, and it is these amino acids that are highly conserved when comparing Ig domains to each other. What might be the advantage of this structure for use as antibody variable domains?

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The Answer of Each immunoglobulin (Ig) domain is composed of a structure known as a '$\beta$-sandwich,' which consists of two $\beta$ sheets covalently linked by a disulfide bond. Only a subset of the ~110 amino acids in each domain are required to establish this overall structure, and it is these amino acids that are highly conserved when comparing Ig domains to each other. What might be the advantage of this structure for use as antibody variable domains?

Each Immunoglobulin (Ig) Domain Is Composed of a Structure Known β\betaβ

Each Immunoglobulin (Ig) Domain Is Composed of a Structure Known $\beta$