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This review will focus on α-helical protein assembly motifs where the α-helix is the major element of secondary structure involved in the folding and stability of the structure and may also be involved in function by binding to receptor molecules. Apart from the three types of α-helical motifs discussed, i.e. those motifs that form autonomously folded protein domains; those motifs that only form a stable folded domain when dimerized; and a motif that requires other structural elements to contribute to the hydrophobic core to stabilize a folded domain, we will present examples of more complex protein assemblies that have combined two different motifs to form a functional molecule.
Kohn et al. (Wed,) studied this question.
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