Different folding options for a protein?

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Discussion Overview

The discussion centers on whether a single protein can adopt different folding configurations that enable distinct functions within an organism, while still maintaining active and inactive states. Participants explore examples and implications of such folding variations.

Discussion Character

  • Exploratory
  • Technical explanation
  • Conceptual clarification

Main Points Raised

  • One participant inquires about the ability of a single protein to assume different folds for various functions, while retaining active and inactive states.
  • Another participant cites functional prion proteins, particularly those from yeast and related fungi, as examples of proteins that can exhibit different folds.
  • A suggestion is made to explore the website Foldit, which gamifies protein folding, indicating that it may provide insights into the folding process.
  • Motor proteins are proposed as fulfilling the conditions of having different conformations that perform various functions, with references to their movement and active sites.
  • Examples of proteins involved in membrane fusion during vesicle release are discussed, highlighting the complexity of their interactions and conformational changes in response to calcium ions.
  • Clathrin is mentioned as a flexible protein that participates in vesicle formation by adopting various shapes and binding with other proteins.
  • Enzymes that move along DNA or RNA are suggested as potentially changing conformation during their activity, though uncertainty remains about the specifics of these changes.

Areas of Agreement / Disagreement

Participants express a range of ideas regarding protein folding and functionality, with no clear consensus reached on specific examples or mechanisms. Multiple viewpoints and examples are presented without resolution.

Contextual Notes

Some claims depend on the definitions of protein folding and functionality, and there are unresolved questions regarding the mechanisms of conformational changes in certain proteins.

Who May Find This Useful

This discussion may be of interest to those studying protein biology, molecular biology, or biochemistry, as well as individuals exploring the practical aspects of protein folding through platforms like Foldit.

icakeov
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Hello, I was wondering whether one same protein can assume different foldings that can do different functions in the organism? (each folding still having the usual active/inactive state)

And if the is a specific example for this?

Many thanks for any thoughts!
 
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Have you been to https://fold.it yet? You may find that folding proteins is fun and challenging.
 
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icakeov said:
assume different foldings that can do different functions in the organism? (each folding still having the usual active/inactive state)
I think, generally, motor proteins fulfill your conditions.
As they move back and forth (different conformations), they will be doing functions (moving things or different steps in the overall movement cycle), and to some degree maintain their active sites (binding sites?).
An example is the http://muscle.ucsd.edu/musintro/bridge.shtml.

Another similar example could be proteins involved in membrane fusion during vesicle release in response to calcium ions entering a nerve terminal.
Go to SNARE protein and pore formation in this link.
This is a complex system with many parts binding other parts at different times during the process (which has a lot of other steps in addition).

Going the opposite way (from the membrane's point of view), clathrin is involved in vesicles pinching off from a membrane sheet. These molecules are flexible (implying a continuum of shapes) and bind to themselves and other proteins in order to form vesicles.

Another possible group could be enzymes moving along a linear molecule like DNA or RNA. I am guessing these are changing conformation as they cycle along, but I don't really know for sure.
 
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Super helpful responses! Thank you so much!
 

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