The goal of Dynameomics is to perform atomistic molecular dynamics (MD) simulations of representative proteins from all known folds in explicit water in their native state and along their thermal unfolding pathways. We began by creating a Consensus Domain Dictionary---a list of metafolds for systematic coverage of fold space. From this analysis there are 1695 unique protein fold families and a target, or representative, was chosen from each. Only 807 of these targets represent ‘simulatable’ protein, autonomously structured, folds, which has implications for the use of domain dictionaries in bioinformatics. Simulation of these targets has been completed and will be discussed here. The behavior of several specific targets is highlighted to illustrate some of the general properties in the full data set and to demonstrate the role of MD in understanding protein function and stability. To encourage understanding of the relationships between protein dynamics, function and disease, we have constructed a web site, complementary to the PDB, which allows access to a novel hybrid relational/multidimensional database to view and interrogate simulations of the Top 100 targets: http://www.dynameomics.org. We, and others, are now mining the Dynameomics database in an attempt to determine the general rules governing protein folding and kinetic stability, which should aid in deciphering genomic information and for protein engineering and design.