Biochemistry, Biophysics & Structural Biology-Department of Biological Sciences - Carnegie Mellon University

Biochemistry, Biophysics, and Structural Biology

Eric T. Ahrens

Professor

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

Affiliated Biological Sciences Faculty

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.
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Marcel P Bruchez

Associate Professor

The Bruchez Group studies the dynamics of translation and co-translational regulation of protein synthesis and folding using single molecule biophysical measurements.
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Alex Evilevitch

Affiliated Biological Sciences Faculty

Our group uses biophysical approaches in order to learn about the fundamental physical principles that control viral genome encapsidation and release as well as capsid stability. This research program takes advantage of the high-resolution cryo electron microscopy, AFM, light scattering and microcalorimetry. Furthermore, our findings provide tools for the rational design of therapeutic agents that selectively interfere with the encapsidation process, and in addition tools to improve encapsidation in vitro in order to make stable vectors for gene delivery.
Webpage, Laboratory Webpage, Group Website

David D. Hackney

Professor

Research focuses on the investigation of the biochemical and biophysical properties of biological molecular motors, both in free solution and at the single molecule level. This includes studies of the mechanism and regulation of kinesin superfamily members, helicases and other ATPases.
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Chien Ho

Professor

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.
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Frederick Lanni

Associate Professor

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

Associate Professor

Research in the Lee lab focuses on the structure and function relationship of the mammalian endoplasmic reticulum. We apply biochemical and imaging approaches to investigate this question in cultured cells.
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Adam D. Linstedt

Professor

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.
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A Javier López

Associate Professor

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.
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Mark R. Macbeth

Assistant Professor

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.
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Jonathan S. Minden

Professor

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.
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Manojkumar A. Puthenveedu

Assistant Professor

The biochemical mechanisms underlying the trafficking of signaling receptors are the main interest of the Puthenveedu laboratory. We focus on trafficking events that regulate signaling by G protein-coupled receptors involved in drug addiction.
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Gordon S. Rule

Professor

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.
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Russell S. Schwartz

Professor

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.
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Alan S. Waggoner

Maxwell H. and Gloria C. Connan Professor of Life Sciences

Research has focused on the development of fluorescence-based detection systems for biology and biotechnology. Our current focus applies the Fluorogen-Activating Protein (FAP) technology to develop novel biosensors of protein interactions and pathway regulation within living cells.
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John L. Woolford

Professor

Having developed methods to purify ribosome assembly intermediates, the Woolford laboratory is now mapping ribonucleoprotein neighborhoods within assembling ribosomes. We have developed assays to identify protein-protein as well as protein_RNA contacts within assembling ribosomes. Based on structure predictions, mutations are being constructed to disrupt these interactions, to evaluate their importance in ribosome assembly and function.
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