David Baker, a computational biochemist and lead author of the work, is revolutionizing science with his team. They have utilized new computational and genomic technologies to determine how amino acids fold into protein structures that are the building blocks of life, a major new achievement.
Scientists have understood that proteins formed a 3D structure based on its amino acid sequence since the 1960s. However, it’s not known how to predict exactly what structure proteins will fold into based on their sequence alone.
Protein structure can be determined using several techniques like nuclear magnetic resonance and x-ray crystallography. But of the millions of known proteins, only about 110,000 are contained in the international repository of such data, the Protein Data Bank. That detail of knowledge about a protein can be critical to knowing its function, making it very important to biologists and chemists.
“The most brilliant thing David has done is build a community,” Neil King, a former postdoctoral fellow in Baker’s lab, and currently an investigator at UW’s Institute for Protein Design (IPD), told Science.
Rosetta has limitations, and sometimes has struggled with accurately predicting the structure of larger proteins. “I wasn’t sure whether I would get there,” Baker said, “I don’t feel that way anymore.”
He was inspired by work done in the 1990s, when computational biologist Chris Sander, then with the European Molecular Biology Laboratory in Heidelberg, Germany, and now with Harvard, suggested that DNA sequences might help identify amino acids that would naturally pair together when proteins folded up.
Aside from looking at existing proteins, Baker wants to make proteins for a purpose. “We were limited by what existed in nature...we can now short-cut evolution and design proteins to solve modern-day problems,” he explains, “we can now build a whole new world of functional proteins.”
Sources: Science