Can you please briefly define these five classes of domain folds.: α, β, α / β, α + β, and cross-linked domains, and compare/contrast the four helix-bundle and the globin fold?
Can you please briefly define these five classes of domain folds.: α, β, α / β, α + β, and cross-linked domains, and compare/contrast the four helix-bundle and the globin fold?
On a larger scale based on α and β secondary structures, the classes of domain folds are:-
1. α: In this structural domain there are all α proteins and they form a tertiary structure composed entirely of α-helices predominantly (exception: a few isolated β sheets on the periphery may be present).
2. β: In this structural domain there are all β proteins and they form a tertiary structure composed entirely of β-sheets predominantly (exception: a few isolated α-helices on the periphery may be present).
3. α / β: Here the α+β protein both are preset to form the tertiary structure, the α-helices and β-sheets (mostly antiparallel) occur alternatively here along the backbone.
4. α + β: Here the α+β protein both are preset to form the tertiary structure, the α-helices and β-sheets (mostly antiparallel) occur separately here along the backbone.
5. Cross-linked domains: Here the amino acid functional groups of the protein polypeptide chain are chemically joined via two or more molecules by a covalent bond i.e the molecules are cross-linked.
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