Gerlt Receives Arthur C. Cope Scholar Award
John Gerlt, the Gutgsell Endowed professor of biochemistry at the University of Illinois at Urbana-Champaign School of Molecular and Cellular Biology, has been selected by the American Chemical Society as one of 10 national candidates to receive an Arthur C. Cope Scholar Award.
Gerlt received the award for his research leading to a deeper understanding of how enzymes accelerate a wide range of reactions and develop different mechanisms. His work has included pioneering studies of how enzymes, such as mandelate racemase, abstract protons from extremely weak acids to generate carbanion intermediates. Gerlt and co-workers also suggested that electrophilic catalysis and strong hydrogen bonding were key factors in making such difficult reactions proceed at reasonable rates. These studies have led to a better appreciation for the sophisticated tools enzymes can use to accelerate reactions.
Currently, Gerlt is studying two groups of enzymes that are derived from common ancestors, both of which share the ubiquitous (β/α)8-barrel fold: the members of the enolase superfamily and the members of the orotidine 5’-monophosphate decarboxylase suprafamily.
Photo credit to L. Brian Stauffer, University of Illinois, Urbana-Champaign.
Gierasch Garners Dorothy Crowfoot Hodgkin Award
Lila M. Gierasch, professor of biochemistry and molecular biology at the University of Massachusetts, Amherst, will receive the Protein Society’s 2010 Dorothy Crowfoot Hodgkin Award at the society’s annual symposium in August.
According to the Protein Society, the award, sponsored by Genentech, is granted “in recognition of exceptional contributions in protein science, which profoundly influence our understanding of biology.” Gierasch received the award in recognition of her exceptional contributions to the understanding of biology through the application of biophysical methods to interrogate biological systems.
Gierasch’s research has had a major impact on fields spanning sequence-structure relationships, protein folding and aggregation, the pioneering application of novel biophysical analyses, (principally NMR), molecular recognition and cooperativity in molecular machines and protein secretion. Her most recent research focuses on the chaperone-mediated folding process, how a β-sheet “clam” protein is folded and how to monitor protein folding in a living cell and compare it with in vitro folding.
Orth Wins Award in Chemical Research
Kim Orth, associate professor of molecular biology at the University of Texas Southwestern Medical Center, was honored with the 2010 Norman Hackerman Award in Chemical Research for her pioneering work on the mechanisms bacteria use to cause disease.
The Welch Foundation, one of the nation’s oldest and largest sources of private funding for basic research in chemistry, presents the annual award to honor up-and-coming scientists at Texas institutions. Recipients are recognized for expanding the frontiers of chemistry through their innovative research. First bestowed in 2002, the award pays tribute to the late Norman Hackerman, a noted scientist and longtime chairman of the foundation’s scientific advisory board.
Orth has discovered new mechanisms by which invading bacteria hijack and deregulate a cell’s signaling systems, cutting off the cell’s ability to communicate with other immune-system cells that are needed to fight off disease. Her studies also have uncovered previously unknown mechanisms human cells use to carry out normal functions. For example, she discovered that an infectious ocean-dwelling bacterium found in oysters and other shellfish kills its host’s cells by causing them to burst, providing the invader with a nutrient-rich meal that can then be used to fuel proliferation. The invading pathogen overtakes the host’s autophagy machinery, a process that is usually tightly controlled.