Given that \(\beta\) -strands provide a more genetically economical way for a polypeptide to cross a membrane, why has nature chosen \(\alpha\) -helices as the membrane-spanning motif for G-protein-coupled receptors? That is, what other reasons can you imagine to justify the use of \(\alpha\) -hclices?

Short Answer

Expert verified
The use of \(\alpha\)-helices in G-protein-coupled receptors can be justified due to their robustness, stability in the membrane, facilitation of lipid interactions, and their potential role in transmembrane signal transmission.

Step by step solution

01

Understand the Basic Structures

The basic difference between \(\alpha\)-helices and \(\beta\)-strands is in the protein structures they form. \(\beta\)-strands form a flat, pleated sheet while \(\alpha\)-helices form a coiled spring-like structure. The form of these structures affects how they function within a protein.
02

Understanding the Function of G-Protein-Coupled Receptors

G-protein-coupled receptors (GPCRs) are a large protein family of receptors that detect molecules outside the cell and activate internal signal transduction pathways. They are involved in a wide range of physiological processes. They are seven-transmembrane domain proteins that traverse the membrane seven times, typically in the form of \(\alpha\)-helices.
03

Reasons for using \(\alpha\)-helices

Some of the reasons for using \(\alpha\)-helices might include their overall robustness and stability. The coiled shape forms a 'tube' through the membrane, which can be more stable and less likely to cause leakage. Also, the specific form of an \(\alpha\)-helix may facilitate the interaction with lipids in the membrane. Transmembrane communication could be another reason; the \(\alpha\)-helices could provide a mechanism for transmitting signals across the cell membrane.

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