Different folding options for a protein?

In summary, proteins can assume different foldings that can perform different functions in an organism, while still maintaining their active/inactive state. One example of this is functional prion proteins found in yeast and related fungi. Motor proteins, such as those involved in muscle movement, also fulfill these conditions as they adopt different conformations while carrying out their functions. Other examples include proteins involved in membrane fusion, such as SNARE proteins and clathrin, and enzymes that move along linear molecules like DNA or RNA.
  • #1
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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  • #3
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!
 

1. What is the significance of different folding options for a protein?

The folding of a protein is crucial for its structure and function. Different folding options can result in different shapes and ultimately determine how the protein interacts with other molecules in the body.

2. How are different folding options for a protein determined?

The folding of a protein is determined by its amino acid sequence, as well as external factors such as temperature, pH, and the presence of other molecules. Additionally, chaperone proteins can help guide the folding process.

3. Can a protein have multiple folding options?

Yes, a protein can have multiple folding options, which may be influenced by external factors. This allows for the protein to have different functions and interactions in different environments.

4. What are the consequences of incorrect folding options for a protein?

If a protein does not fold correctly, it may not be able to perform its intended function. This can lead to a variety of consequences, including diseases and disorders.

5. How do different folding options affect the stability of a protein?

The stability of a protein is dependent on its folding. Different folding options can result in varying levels of stability, which can impact the protein's ability to perform its function and potentially lead to degradation or denaturation.

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