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Andrei Lomize has a research background in computational modeling, theoretical analysis of protein structure, folding, stability, and interactions. He has developed computational methods, software, and empirical energy functions and bioinformatics resources to tackle a variety of problems, including conformational analysis of peptides, NMR spectroscopy data, and thermodynamics related to helix-coil transitions in micelle and protein environments. His research has focused on the impact of mutations on protein stability, energetics, and protein-lipid interactions, particularly in calculating free energies associated with α-helix association in lipid bilayers. He is the principal author of bioinformatics resources such as the Orientations of Proteins in Membranes (OPM) database and the Positioning of Proteins in Membranes (PPM) web server, and has participated in NMR studies of membrane peptides and proteins. With over 45 published papers in peer-reviewed journals and book chapters, he has also engaged in the Critical Assessment of Techniques for Protein Structure Prediction (CASP) and GPCR structure modeling and docking experiments.
UM College of Pharmacy • Ann Arbor, MI
Conducts research on computational modeling and protein interactions.
Department of Electrical Engineering and Computer Science