Professor Bowler is engaged in research on protein folding and biological electron transfer. The focus in protein folding is on the properties of denatured proteins and how these properties affect the early events in the folding process. Work on electron transfer emphasizes how protein dynamics modulates electron transfer rates.
Professor Briknarová uses nuclear magnetic resonance (NMR) spectroscopy, biochemical and biophysical techniques to study the structure, function and dynamics of biological macromolecules. A question of particular interest is how cell identity is established and maintained at the molecular level.
Professor Hill's laboratory studies ribosome structure, function and dynamics using a wide range of methods, including time-resolved quench-flow techniques aimed at characterizing the structural changes that occur during protein synthesis.
Professor Layton is investigating the role that nanoscale biomechanics plays in predicting the fate of organisms under a variety of environmental stresses. Model organisms that he is studying include Arabidopsis thaliana and Trichodesmium erythraeum. He is also working on a formal relationship between anthropogenic entropy acceleration and information.
We are investigating how the structure of HIV RNA regulates viral replicative processes including translation of viral proteins, encapsidation, splicing, and RNA dimerization.
My laboratory is devoted to understanding structure/function relationships in proteins. There are three current areas of biochemical research. (1) We study the prion protein, the causative agent of infectious amyloid diseases including scrapie, mad cow disease, and Creutzfeld-Jakob disease. (2) We study how amino acid radicals modulate electron transfer through the polypeptide backbone using the blue copper protein azurin. (3) We study the structure and mechanism of tyramine beta monooxygenase, a copper enzyme involved in neurotransmitter biogenesis.
My research focuses on the application of principles from computer science on problems in biology and biochemistry. The approaches practiced by members of my lab include those drawn from the fields of data mining, evolutionary computation, pattern recognition, artificial intelligence, multivariate analysis, self-evolving Markov models, dynamic programming techniques, simulation, and modeling. We have collaborated on problems in identifying and measuring the similarity of RNA secondary structure, investigating global forces involved in genomic and proteomic evolution, non-alignment techniques in evaluating phylogenetic relationships, and analyzing metagenomic data
The Ross group uses biological fluorescence spectroscopy to investigate protein-protein and protein membrane interactions in initiation of blood coagulation and protein-protein and protein-nucleic acid interactions in regulation of transcription and repair of damaged DNA.
Our goal is to dissect the role of DNA structure, DNA topoisomerases, architectural DNA-binding proteins, alternate sigma factors, and other transcription factors in the regulation of gene expression and the replication of linear DNA in bacteria.
My research is mechanisms of metalloenzymes, characterization of reactive intermediates, activation of dioxygen and organic substrates during enzyme catalysis, proton-coupled electron transfer, use/theoretical interpretation of isotope effects in metabolic and environmental processes.
Our laboratory is interested in the structural biology of cellular signaling through heterotrimeric G proteins. We use the tools of X-ray crystallography, enzymology and molecular biology to explore and understand the structural and chemical mechanisms by which G proteins regulate cellular processes and are themselves regulated.
My research focuses on the mechanism of interaction of metal complexes with biomolecules that can lead to the formation of genetic aberrations such as mutations, cancer and toxicity. My primary metal of interest is chromium, which in the +6 oxidation state, is a known human carcinogen. One method by which chromium may induce cancer in humans is through oxidative damage to nucleic acids. Our research group is focused on the mechanism by which this oxidative chemistry may occur and the resulting lesions that are formed on DNA that can give rise to carcinogenesis.