David Eisenberg
Research Overview
Our lab studies protein interactions using X-ray crystallography, computational analyses, and biochemical methods. We have a long-term goal of understanding and manipulating the functioning of cells through the interactions of their constituent proteins.
X-ray crystallography is a powerful tool for exploring protein structure and interactions. The crystallography projects in our lab fall into two groups. The first focuses on amyloid and prions, classes of pathologically interacting proteins. Our goal is to understand the structures that underlie the pathologies. The second group studies the structural biology of Mycobacterium tuberculosis, with particular focus on protein-protein complexes, as part of the TB Structural Genomics Consortium.
In the computational realm, we aim to infer functional relationships between proteins based on genome sequences and protein expression data. Two methods we have developed are the phylogenetic profile and Rosetta Stone methods, which analyze and compare gene and genome sequences from multiple organisms. In addition, we have built the Database of Interacting Proteins, which serves as a community resource and provides data for benchmarking our computational predictions.
Eisenberg 65th Birthday Symposium • More • Group Photos From 2007
