Daniel Herschlag, professor of biochemistry, chemistry and chemical engineering at Stanford University, has been awarded the 2010 American Society for Biochemistry and Molecular Biology William C. Rose Award in recognition of his outstanding contributions to biochemical and molecular biological research and a demonstrated commitment to the training of younger scientists.
Herschlag will present an award lecture titled “How Enzymes Work” at 8:30 a.m. Tuesday, April 27, at the 2010 annual meeting in Anaheim, Calif.
Integrating concepts and techniques from physics, chemistry and biology, Herschlag and his lab team seek to unlock the fundamental behaviors of RNA and proteins and, in turn, how these behaviors determine and affect biological processes. Herschlag is perhaps most famous for his groundbreaking research in RNA structure, folding and catalysis, particularly his discoveries concerning the mechanisms and thermodynamics of group I and hammerhead ribozymes.
“Herschlag has set the standard for excellence in this field,” notes colleague Carol A. Fierke, chairwoman of the University of Michigan’s department of chemistry. “His studies using single-atom substitution and kinetic analysis to identify metal binding sites in ribozymes are a tour de force. Additionally, [he] provided the first direct demonstration of the role of binding interactions in chemical catalysis in ribozymes; these studies elegantly demonstrated the role of binding energy in stabilizing both ground-state and transition-state interactions.”
Of course, as Fierke and others will point out, ribozymes represent just a portion of Herschlag’s superb body of research. He is also one of the foremost experts on the mechanisms of both naturally occurring and enzyme-catalyzed phosphoryl transfer reactions and a leader in advancing research into RNA chaperones. He has provided tremendous insight into the general nature and evolution of enzyme catalysis.
In this latter area, Herschlag is well known for identifying the implications of a property he termed “catalytic promiscuity”— in which proteins in the same superfamily often display low levels of activity toward reactions catalyzed by other members within the superfamily— for the evolution and design of new enzymes.
In addition to his scientific contributions in the fields of RNA, enzymes and RNA enzymes, Herschlag also has demonstrated an equal level of commitment to training younger scientists. Says Rick Russell, associate professor of chemistry and biochemistry at the University of Texas and former postdoctoral fellow in Herschlag’s lab, “Dan has been committed to doing everything necessary to mentor his group members at the highest possible level in all aspects of training, from designing and interpreting the experiments to preparing the presentation.”