It all happens in a femtosecond – a quadrillionth of a second.
That's the time an enzyme needs to shape-shift into its most
reactive form, trigger a chemical reaction and snap back into
its original shape. We can now enter this high-speed world to
interrupt the chemical reactions that sustain some of our
deadliest pathogens and cause disease. Doing so could lead to
antibiotics that won't trigger bacterial resistance. In 1946,
Nobel laureate Linus Pauling suggested that enzymes are most
active during fleeting transition states, but only recently has
Vern Schramm at the Albert Einstein College of Medicine in
Yeshiva University, New York, moved the science from the
blackboard to the clinic. "The problem in this whole field has
been no one really knew what the structure of an enzyme's
transition state looked like," he says. "It's hard to see
something that has [effectively] no lifetime." Over the course
of a decade, Schramm has reconstructed those states, using
computational and molecular modelling techniques. He