How to resolve AdBlock issue? His world is picoseconds, trillionths of seconds; too short for any atomically resolved experiments: Professor Leonid Zhigilei is a materials scientist at the University of Virginia (USA). He was awarded the Humboldt Research Award for his calculations on the production of nanoparticles and will be spending his associated research stay in Technical Chemistry I at the University of Duisburg-Essen (UDE) in Germany. The focus will be on materials for catalysis.
Catalysts make our high standard of living possible, and the "Energiewende" would be inconceivable without them: They are essential in fuel cells, enable the green production of hydrogen, and also its conversion into storable chemicals as an energy reservoir. For this purpose, catalysts have so-called "active sites": millions of tiny pores in the material into which precursors migrate. There, they convert into a product of interest – without a catalyst, this would happen more slowly, with more energy input, or simply not at all. Therefore, the active sites must be easily accessible and not blocked by foreign molecules. 
Such pure nanoparticles for catalyst materials can be produced by high-energy laser pulses, as the team of Technical Chemistry I at UDE does. To further understand these processes and improve them accordingly, it is necessary to study the individual steps – but that is not possible even with high-tech methods in experiments; they just happen too quickly.
Leonid Zhigilei, on the other hand, uses supercomputers to simulate these steps with atomic resolution and calculates the ultrashort time scales: "We design theory and experiment together. That way, my simulations can show both dead ends and promising changes in advance."
Zhigilei is already cooperating with the Technical Chemistry I team led by Professor Stephan Barcikowski. As soon as the situation will allow, he is going to spend a longer period of time as a guest in the working group. "We do research in different fields, and that's exactly why our collaboration is so fruitful," says Zhigilei, explaining his decision to come to UDE after receiving the Humboldt Research Award. "We ask each other questions that the other would not have thought of."
The Humboldt Research Award is granted to leading researchers from all disciplines outside Germany. It recognizes their accomplishments and enables them to spend several months researching an academic institution in Germany.
A team from Japan and the United States has identified the design principles for creating large "ideal" proteins from scratch, paving the way for the design of proteins with new biochemical functions.
The team had previously developed principles to design small versions of what they call "ideal proteins," which are structures without internal energetic frustration.
Such proteins are typically designed with a molecular feature called beta strands, which serve a key structural role for the molecules. In previous designs, the researchers successfully designed alpha-beta proteins with four beta-strands.
"The ideal proteins we have created so far are much more stable and more soluble than proteins commonly found in nature. We think these proteins will become useful starting points for designing new biochemical functions of interest," said co-first author Rie Koga, a researcher in Exploratory Research Center of Life and Living Systems of Japan's National Institutes of Natural Sciences (NINS). 
The team found that while the designed proteins were structurally ideal, they are too small to harbor functional sites.
"We set out to test the generality of the design principles we developed previously by applying them to the design of larger alpha-beta proteins with five and six beta-strands," said co-first author Nobuyasu Koga, associate professor in the Institute for Molecular Science of NINS.
The results were puzzling. They found that their experimental structures differed from their supercomputer models, resulting in proteins that folded differently by swapping the internal locations of their beta-strands. The team struggled with the strand swapping puzzle, but by iterating between computational design and laboratory experiments, they concluded.
"We emphasize that experimental structure determination is important for iterative improvement of computational protein design," said co-first author Gaohua Liu, chief scientific officer of Nexomics Biosciences.
"Sometimes we learn the most from these ideal proteins when their experimental structures differ, rather than match, their intended design, since this can lead to a deeper understanding of the underlying principles", added Gaetano Montelione, co-author and professor of chemistry and chemical biology at Rensselaer Polytechnic Institute.
The reason for the strand swapping, they determined, was due to the strain of the whole system on the foundational backbone structure. According to Nobuyasu Koga, the strain is global, instead of connection to connection. Proteins can adjust the length and register of strands across the system to alleviate this backbone strain.
Next, the researchers plan to continue studying the trade-off between more functional proteins with what could be considered less-than-ideal qualities.
"We would like to design proteins with more complex functional sites by incorporating non-ideal features such as longer loops, which are important not only for function but also for relieving global backbone strain," said David Baker, co-author, and professor of biochemistry at the University of Washington.
