Scientists at UCSB, as part of a larger international research collaborative, have recently developed a better understanding of the process of protein folding of chains of amino acids.

Protein folding, which happens in virtually all of our cells, determines the shape the protein chain will take and ultimately what functions they will perform in the body. As a result, unfolded strands of linked amino acids begin rapidly folding into various forms to produce hormones, enzymes and muscles.

The team’s findings were published in the Proceedings of the National Academy of Sciences and have garnered attention due to the important nature of protein folding in many organisms.

“The protein folding process is the final step in the assembly of molecules capable of performing certain tasks; these molecules are the first things that are unique to life, going up in scale” experimental biological physics professor Everett Lipman, co-author of the study, said.

During the folding process, two types of friction affect the final outcome: the internal friction within the protein and the external friction of the protein moving through its surrounding environment.

According to professor Kevin Plaxco, who has been studying protein folding for over 15 years, the study has shed light on the role and magnitude of this friction during the folding process.

“Surprisingly, that internal friction is very small; it’s so small that people have been arguing about whether or not it even exists,” Plaxco said.

However, according to Lipman, the formation rate is affected by other factors.

“Everything is vibrating because it has some temperature, and if you are very small, the random motions of the fluid, like those random vibrations, are very big compared to your average motion through the fluid,” Lipman said. “Every time you try to go somewhere, you’re banging into things with masses comparable to yours moving in random directions, so when you try to develop some sort of directed motion, it is very quickly counteracted by all these things smacking into you at random.”

Consequently, this research has the potential to help scientists more accurately predict the fate and final form of unfolded protein strands.

“One goal of studying protein folding would be to understand from the sequence what the shape [of the protein] is going to be and then from the shape what the function is going to be,” Lipman said.

Scientists remain hopeful that in the future, these findings, which may serve as the basis for future research on this little-known process, could help them learn how to manipulate the shaping and folding processes in order to produce a certain desired outcome.