Why g-proteins has a shape of a helix?

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    Helix Shape
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Discussion Overview

The discussion centers around the structural shape of G-proteins, specifically why they adopt a helical conformation. Participants explore the implications of this structure in relation to stability and function within cellular membranes.

Discussion Character

  • Exploratory, Technical explanation, Conceptual clarification

Main Points Raised

  • One participant questions the reason behind the helical shape of G-proteins.
  • Another participant provides links to images that may illustrate the structure of G-proteins.
  • It is suggested that G-proteins are embedded in membranes, which influences their stable structure.
  • One participant argues that the helical conformation is the most chemically stable form for the protein and raises the point that the more relevant question is why this structure benefits G-protein function.
  • Another participant mentions that hydrophilic amino acids can orient inwards in a beta-sheet, which may complicate the shielding effect compared to a helical structure.

Areas of Agreement / Disagreement

Participants present various perspectives on the reasons for the helical shape of G-proteins, and while some points are aligned, there is no clear consensus on the primary advantages or implications of this structure.

Contextual Notes

The discussion does not resolve the underlying assumptions about the stability and functional advantages of helical versus other protein structures, nor does it clarify the specific conditions under which these structures are advantageous.

nemzy
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does anyone know why g-proteins has a shape of a helix??
 
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G-proteins are stuck in membranes, thus they have a structure that allows them to be most stable.
 
It's just the most chemically stable conformation of the protein. In a way, the question is asked a bit backward. The important question isn't why a g-coupled protein would form a helix, but why a helical structure would be advantageous to the function of a g-coupled protein. The simplified answer to that question is that it allows the hydrophobic region of the protein to interact with the hydrophobic cell membrane.
 
Yes, the hydrophilic amino-acids can turn inwards of the helix in a beta-sheet such shealding is difficult.
 

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