Biochemistry, Biophysics, and Structural Biology

Eric T. Ahrens
Using MRI-based biophysical measurements, the Ahrens laboratory focuses on the elucidation of development and pathology of the central nervous system.

Bruce Armitage
The Armitage group synthesizes peptide nucleic acids (PNAs) that bind to specific DNA or RNA targets. The ultimate goal is to efficiently block gene expression by interfering with transcription or translation.

Peter B. Berget
The Berget group purifies and characterizes modified single chain variable fragment antibody molecules that activate fluorogens. These molecules are engineered to be biosensors that respond to primary sequence modifications such as phosphorylation, methylation and proteolysis.

David D. Hackney
Research focuses on the investigation of the biophysical properties of the movement produced by molecular motors at the single molecule level. Kinesin superfamily members and the coupling of ATP hydrolysis to the conformational and binding changes that produce motility by molecular motors are major foci.

Chien Ho
The Ho laboratory focuses on determining the structure of hemoglobin in solution at atomic resolution using multinuclear NMR spectroscopy. Research centers on study of both normal and mutant human hemoglobins to understand the molecular mechanism of transporting oxygen from the lungs to tissues.

Frederick Lanni
The Lanni group is interested in cellular biophysics, particularly mechanics analysis of fibroblast cytoskeletal function.

Adam D. Linstedt
Investigating molecular mechanisms that establish and maintain the membrane-bounded compartments of the secretory and endocytic pathways is the focus of the Linstedt laboratory. Approaches include permeabilized cell assays, biochemical reconstitutions, cell imaging techniques, and molecular genetic experiments.

A. Javier López
Projects in the López laboratory use various model systems to study how splicing of pre-mRNA is regulated in vivo and how alternative splicing influences development and cellular function. Recursive splicing mechanisms and their role in expression of very large transcription units are major areas of investigation.

Mark R. Macbeth
The Macbeth lab is interested in RNA-protein interactions, specifically those that involve ADARs, or Adenosine deaminases that act on RNA. We use structural, biochemical and genetic methods to characterize the 3-D ADAR structure, its enzymatic mechanism, and the regulation of its activity.

Jonathan Minden
The Minden Lab is developing new tools for comparative proteomics. These methods allow us to quickly detect and identify protein changes during development and between healthy individuals and those with specific illnesses.

John F. Nagle
Studies in the Nagle laboratory are aimed at developing a new method to study membranes using diffuse x-ray and neutron scattering.

Gordon S. Rule
NMR methods are being used to investigate the role of protein dynamics in enzymatic function. Current systems under study in the Rule laboratory include cellular detoxification enzymes (glutathione transferases) and Eco RV endonuclease. In addition, the enzymatic mechanism of glutathione transferases is being investigated using site-directed mutagenesis, NMR spectroscopy, and X-ray diffraction.

Russell Schwartz
Research in the Schwartz group is centered on developing computational models, algorithms, and data structures for simulating biological self-assembly, and applying them to systems that include cytoskeleton dynamics and virus capsid assembly.

Alan Waggoner
Research in the Waggoner laboratory focuses on the development of fluorescence-based detection systems for biology and biotechnology. These include fluorescent probes and imaging microscopes for studying protein and nucleic acid regulatory pathways in living cells and tissues.

John Woolford
Having developed methods to purify ribosome assembly intermediates, the Woolford laboratory is now mapping ribonucleoprotein neighborhoods within assembling ribosomes.