Andrew Miranker received his bachelors degree in 1986 from Carnegie-Mellon University. From Pittsburg, he pursued his dissertation in biophysics in the laboratory of Professor Martin Karplus at Harvard University, Dept. of Chemistry. There, he evaluated the physical basis of molecular recognition through the development of tools for computer aided drug-design. These tools included small molecule docking algorithms as well as a computational alchemical approach to de novo prediction of molecules complementary to macromolecular surfaces. Dr Miranker completed his dissertation in 1992 and traveled abroad to the University of Oxford, UK. As a NATO fellow, and Junior Research Fellow of Christ Church, Dr Miranker investigated globular protein folding using spectroscopic and hydrogen exchange techniques. These studies identified the importance of sub-domains to protein folding pathways and saw the development of novel applications of hydrogen exchange particularly through the use of native state electrospray mass spectrometry. This work was accomplished under the guidance of Professor Christopher M. Dobson at the Oxford Centre for Molecular Sciences. Dr Miranker joined the faculty of Molecular Biophysics and Biochemistry at Yale University in the fall of 1997. There he has established an independent laboratory which focuses on experimental and computational investigations of protein folding, misfolding and pathological protein assembly in human disease.