A recent paper by a group of University of California, Berkeley researchers has been hailed as a major breakthrough in protein biology.
The paper was published in the Proceedings of the National Academy of Sciences.
The team, led by Robert C. Anderson, professor of protein biology at UC Berkeley, identified a protein called T3 that binds to the surface of proteins and blocks them from folding into larger structures.
This allows proteins to be broken down into smaller pieces, the researchers say.
The group is working on a series of proteins that could be used to make more complex protein structures.
The study shows that the surface-bound T3 protein is a critical building block for protein folding.
But what the researchers don’t know is whether the T3 binding to the protein is the same binding that other proteins have to their surface.
In this way, it is possible to make proteins that fold into more complex structures, such as proteins that make up cell membranes.
“We wanted to explore whether we could make a protein that has a very similar binding to its surface to other proteins and that we could understand how that binding interacts with the binding of other proteins,” Anderson told Business Insider.
“It was a really challenging problem, because it’s not really understood.
So, the idea of making a protein with the same surface-binding ability as other proteins was really appealing.”
The research team, which included Anderson and colleagues from the National Institutes of Health, also found a protein whose surface-to-surface binding to T3 was not the same as another protein that is part of the same family of proteins.
This protein was called T6.
The researchers named this protein T6c, and the protein binds to T6 through a different mechanism than T3 does.
This new understanding of how the surface binding of protein proteins works may allow researchers to create proteins that bind to their own surface without being bound by the binding between the proteins.
The scientists are now working on building a protein molecule that has the same receptor-binding abilities as the T6 protein, but without the binding.
They are also working on another protein molecule with the receptor-binding ability of the T5 protein.
The team is currently developing the new protein molecules.
“There’s a lot of work to be done,” Anderson said.
“This is the first time we’ve shown a mechanism by which a receptor can bind to its own surface, and we’ve done that without any other binding.
We are going to need a lot more work to understand this.”
The researchers say that by combining their protein structures, they could be able to make a new type of protein.
Anderson said that the group’s findings will help researchers understand how proteins work and where proteins bind to each other, and that they could make new proteins that are more complex and perform better in a variety of situations.
“One of the things we’ve learned about proteins is that they’re very modular, and they can change their structure at any time,” Anderson explained.
“And so, this is a very good opportunity to make an entirely new protein with these new structural characteristics.”
Anderson and his colleagues are currently studying the structure of proteins, including the structures of the building blocks that make them up.
The structures of proteins have been known for a long time, but the research has not been able to pinpoint exactly what makes them different.
They said that by finding the structure that binds at the surface and that is able to bind to other protein molecules, they hope to understand how protein structures work in more detail.
“The goal is to understand the molecular mechanism that drives the binding at the cellular level,” Anderson added.
“That would allow us to design a protein structure that is capable of interacting with other proteins.”
The work was supported by the National Science Foundation and the National Center for Biotechnology Information.