Georg Hochberg

Research Area

Cells are filled with a dazzling diversity of proteins that can seem exquisitely tuned to their functions. How did evolution produce this diversity? Is it the result millions of years of fine-tuning, or does it reflect a more erratic process that tends to produce Rube Goldberg-like machines replete with gratuitous complexity? Our lab tackles these questions using the evolution of protein complexes as our model system. We use ancestral sequence reconstruction to resurrect long extinct protein complexes and characterize their structure and function using a combination of high-resolution biophysical techniques and high-throughput characterization of protein libraries.

Expertise

Evolutionary biology
Protein complexes
Biophysics
Ancestral sequence reconstruction
Phylogenetics

Recent Publications, Last 3 Years

1. Malay, A.D., Miyazaki N., Biela, A., Chakraborti, S., Majsterkiewicz, K., Stupka, I., Kaplan, C.S., Kowalczky, A., Piette, B.M.A, Hochberg, G.K.A., Wu, D., Wrobel , T.P., Fineber, A., Kuwask, M.S., Kelemen, M., Vavpetic, P., Pelicon, P., Kukura, P., Benesch, J.L.P., Iwasaki, Heddle, J.G. (2019)
An ultra-stable gold-coordinated protein cage displaying reversible assembly. Nature, 569, 438-44

2. Hochberg G.K.A.*, Shepherd, D.A. *, Marklund, E.G. *, Santhanagoplan, I., Degiacomi, M.T., Laganowksy, A., Allison, T.M., Basha, E., Marty, M.T., Galpin, M.R., Struwe, W.B., Baldwin, A.J., Vierling, E., Benesch, J L.P. (2018)
Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions. Science (2018), 359: 930-935. * Equal contribution

3. Hochberg, G.K.A., Thornton, J.W. (2017)
Reconstructing Ancient Proteins to Understand the Causes of Structure and Function. Annu.Rev.Biophys., 22: 247-269. F1000 recommended. DOI: 10.1146/annurev-biophys-070816-033631