Much of the attention paid to this year's Nobel Prize honorees has centered on President Barack Obama being awarded the Nobel Peace Prize. But for a pair of scientists at the University of Pennsylvania, there's an honor that hits much closer to home.
Israeli researchers Gabriel Rosenblum and Ilan Samish — currently post-doctoral students at Penn — came to know biochemist Ada Yonath years ago while studying at Israel's Weizmann Institute of Science in Rehovot. Yonath was awarded this year's Nobel Prize in chemistry for efforts to deduce the structure and function of ribosomes, which act as the cell's protein factory. She shared the prize with two colleagues from America and England.
Rosenblum met Yonath at the beginning of this decade, shortly after what he called "her breakthrough," which involved forming the first high-resolution crystal structures of ribosomes.
"When I first came to her as a master's student, you're basically considered a nobody," said Rosenblum. "You have no skills, you're at the beginning of your way, and she immediately turned away everything she did at that moment and sat with me, giving me 200 percent of her attention," explaining to Rosenblum the details of her findings.
He said that in the late 1970s, Yonath was reading up on polar bears when she noticed that, for the bears to survive during hibernation, there had to be "some kind of mechanism that would preserve the ribosome so they won't fall apart or be degraded by [certain] cellular particles."
What Yonath found is that the ribosomes inside the cells are crystallized, so that only the outer shell of the crystal is exposed; what's inside is protected.
Over two decades, Yonath wrote and published about crystals, all while striving to find the right conditions that allow ribosomes to crystalize so that she could study the three-dimensional shape those crystals take (and thus, the 3-D shape of ribosomes). But it wasn't until 2001 that she was able to X-ray the crystals and study the reflection of the light to finally determine the actual shape the ribosomes took.
"She developed some very general methods that the entire world is using today to find the structures of proteins," said Samish, who knew Yonath through their department at Weizmann.
A Pioneer in Two Fields
Rosenblum pointed out that while Yonath has been noted for her work with ribosome structures, she's also been a pioneer in cryocrystallography — the study of crystals cooled to temperatures below 200° Celsius.
"After she published that, the rest of the world switched to cryocrystallography," said Rosenblum, adding that "within four months, everything changed" as Yonath's methods were adopted across the field.
Her local colleagues observed that the Nobel honor capped an already distinguished career.
"It's really a huge achievement for the Weizmann, for Israel and, of course, for her," said Samish.
For his part, Rosenblum said that "thanks to her, I found this position at Penn," noting that Yonath wrote recommendations for him, and even helped steer him into the field of ribosomes. "I was actually on my way to the West Coast, but I found myself here, thanks to her."