Proteins and Enzymes

ID #1507

Is it possible that the prions are just the thermodynamically favorable resonance structure of the proteins in the brain? In which case the interaction between the two structures would reveal a more stable compound, thus encouraging normal proteins to adopt the prion structure. The only problem with this would be how the prion interacted. Does it create a new pathway like a catalyst or is there some other component of the interaction that I'm not seeing? In summary, I'm not clear on how the normal proteins become prions when a prion is introduced.


In order to replicate, you have to have a "template" to use as instructions, and the tools to make more of the same molecule. In the case of an isolated prion protein, to make more protein (replicate, in this case), you'd need to copy the existing protein. But as we'll see later in the semester, cells have no mechanism for making protein from a protein template. Instead, they have to make protein from an RNA molecule, but prions have no nucleic acid component!

This isn't to say that one misfolded prion protein can't lead to many misfolded prion proteins. Once one "bad" one induces a "good" one to become bad, now there are two bad ones, which then convert another 2. Now you've got 4, then 8, and so on.

Print this record Print this record
Send to a friend Send to a friend
Show this as PDF file Show this as PDF file
Export as XML-File Export as XML-File