Media Coverage

Thomas D. Grant, PhD, research assistant professor of structural biology, has developed a speedy, more precise drug design process called solution scattering.  The process is much faster because it involves using high-intensity X-rays, bypassing the arduous process of crystallizing proteins to learn their structures and then feeding the data into supercomputers. “This is good,” he said, “because we’ll have a lot more capability of curing diseases that haven't been cured, getting rid of side effects that we haven't been able to get rid of with the traditional ways.”

A UB study with Washington University in St. Louis focuses on the construction of antibiotic scaffolds and how new understanding about their nature can help scientists search for new classes of antibiotics through DNA sequencing and genome mining. “The solution of this structure expands on previous discoveries to provide views of the molecular interactions between catalytic domains in a brand new way,” said Andrew M. Gulick, PhD, associate professor of structural biology.

An article on the website of the National Science Foundation reports on new research by Thomas Grant, PhD, research assistant professor of structural biology, that will dramatically improve how scientists “see inside” molecular structures in solution, allowing for much more precise ways to image data in various fields, from astronomy to drug discovery.

UB has received $4.5 million in grants that will help it recruit top scholars and researchers in three specialty fields: robotics, systems pharmacology and X-ray laser technology. UB received three grants from SUNY's Empire Innovation Program, which helps institutions recruit senior faculty members with proven track records. A research consortium funded by the National Science Foundation that's focused on X-ray laser science is one of the beneficiaries.

Research by William L. Duax, PhD, of the Department of Structural Biology, is casting doubt on a commonly held belief about how cells use DNA to make proteins. “There are significant errors in text books. The universal code is not universal and all species now on earth do not use a code ‘frozen in time’ as claimed by Watson and Crick,” says Duax. “Some basic assumptions about evolution are incorrect.”

An article about a study that looked at how the luminescent protein luciferase, found in fireflies and other beetles, produce their color variety quotes Andrew M. Gulick, PhD, assistant professor of structural biology.

Two studies — including one led by Andrew M. Gulick, PhD, associate professor of structural biology — have revealed key operations of nonribosomal peptide synthetases, megaenzymes that bacteria and fungi use to produce peptide natural products.

The Hauptman-Woodward Medical Research Institute (HWI) has added four other life sciences firms into its facility on the Buffalo Niagara Medical Campus. “UB is this large, well-funded entity, the large cruise ship that's going along and we're the little speedboat running alongside. So we can move rapidly into new areas of research and UB offers a fair bit of support,” said Edward H. Snell, PhD.

The University at Buffalo, representing a national consortium of eight research universities and institutes, has been awarded $25 million to transform the field of structural biology and establish the BioXFEL research center, which will be directed by Eaton E. Lattman, PhD, of the Department of Structural Biology.

Eaton E. Lattman, PhD, research professor of structural biology and CEO of the Hauptman-Woodward Medical Research Institute, will direct a major new research center in Buffalo involving a national consortium of scientists.

Timothy C. Umland, PhD, and L. Wayne Schultz, PhD, researchers in the Department of Structural Biology, are using a three-year grant from the Department of Defense to study the relationship between protein interactions and successful host-range expansion in zoonotic viruses that spread from vertebrate species to humans.