Our research focuses on problems at the interface of biophysics and engineering, particularly in understanding the interrelationship between protein structure, molecular recognition and biological function.
Membrane proteins are both fascinating in the wide array of functions they perform, their abundance in the human genome and yet are challenging to work with due to their poor solubility and often low expression. We are interested in developing novel experimental methods to characterize membrane proteins in vivo and in vitro. We use these and other computational and experimental techniques to understand how membrane proteins interact with other proteins and lipids, and how these interactions control biological function.
A number of microorganisms synthesize surface-active agents and use them in a variety of biological processes such as conversion of organic material into metabolically-active components, improving cell motility and formation of biofilms. We are interested in studying the biochemical and material properties of these compounds, and using this information to design biosurfactants with novel chemical properties.
Synthetic biology uses engineering principles to design biological systems with novel functions by combining individual elements (genes, proteins or metabolites) in vitro. We are interested in understanding how these different elements interact (gene transcription, protein-protein interaction, post-translational modifications) and integrating this information to develop models that can be used to design new biological processes. This work is highly collaborative, and we are focusing on developing experimental methods that can be used to increase the molecular diversity of these systems, and applying these methods to engineer new protein functions and interactions.
Berger BW, Kulp DW, Span LM, Billings PC, Bennett JS, DeGrado WF. A consensus motif for integrin transmembrane heterodimerization. (2009) Submitted.
Yin H, Slusky JS, Berger BW, Walters S, Vilaire G, Litvinov RI, Lear JD, Caputo GA, Bennett JS, DeGrado WF. Computational design of peptides that target transmembrane domains. Science (2007) 315: 1817-1822 (doi: 10.1126/science.1136782)
Berger BW, Gendron CM, Robinson CR, Kaler EW, Lenhoff AM. Effects of additives on surfactant phase behavior relevant to bacteriorhodopsin crystallization. Protein Science (2006) 15(12): 2682-2696 (doi: 10.1110/ps.062370506)
Berger BW, Gendron CM, Robinson CR, Kaler EW, Lenhoff AM. The role of protein and surfactant interactions in membrane protein crystallization. Acta Crystallographica D (2005) 61: 724-730 (doi:10.1107/S0907444904029063)
Berger BW, Garcia RY, Lenhoff AM, Kaler EW, Robinson CR. Relating surfactant properties to activity and solubility of the human adenosine A3 receptor. Biophysical Journal (2005) 89(1): 452-464 (doi:10.1529/biophysj.104.051417)
Berger BW, Blamey CJ, Naik UP, Bahnson BJ, Lenhoff AM. Roles of additives and precipitants in the crystallization of calcium- and integrin-binding protein. Crystal Growth & Design (2005) 5(4):1499–1507 (doi:10.1021/cg050013u)