Biologist, Biochemist for Master / Diploma thesis - Genetics, Protein folding in vivo and in vitro
Our lab studies protein folding both in the test tube and in the cell. We aim to understand protein folding well enough to be able to manipulate it. We ask organisms themselves to solve protein folding problems. By examining their solutions we can better understand folding in the cell. We have developed folding biosensors that link protein stability to antibiotic resistance. They enable us to optimize folding in vivo (1) and discover new molecular chaperones (2). Protein folding in the cell is intimately tied to the action of folding catalysts and chaperones. We study the action of these newly discovered folding helpers both in vivo and in vitro using a wide range of genetic, biochemical, biophysical and structural techniques (2,3,4,5,6,7,8). One of these newly discovered chaperones is called Spy (2). Very recently we have uncovered the mechanism by which Spy helps proteins to fold and characterized the structure of an unfolded protein in complex with Spy at an unprecedented resolution. Spy provides an amphiphilic, "folding-friendly" surface that allows its client proteins to fold while bound to the chaperone (5,7,8). Our hypothesis, that other chaperones use a similar mechanism to assist in protein folding, we currently test in our lab on a variety of chaperones.
We have a lot of experience working with German graduate, master and diploma students and can help with the paperwork. Our lab is located at the University of Michigan, one of top five public schools in the country, which provides an excellent research environment.
1. Foit L et al (2009) Optimizing protein stability in vivo. Mol Cell 36: 861-871.
2. Quan et.al. (2011) Genetic selection designed to stabilize proteins uncovers a
chaperone called Spy. Nature Struct. Mol. Biol.18(3):262-9
3. Foit L et al. (2011) Chaperone activation by unfolding. PNAS 110(14):E1254-62.
4. Quan S et al. (2014) Super Spy variants implicate flexibility in chaperone action. Elife.3:e01584.
5. Stull F et al. (2016). Substrate protein folds while it is bound to the ATP-independent chaperone Spy. Nature Struct. Mol. Biol. 23(1):53-8.
6. Docter BE et al. (2016). Do nucleic acids moonlight as molecular chaperones? Nucleic Acids Res. 44(10):4835-45.
7. Horowitz S, et al. (2016). Visualizing chaperone-assisted protein folding. Nature Struct. Mol. Biol. 23(7):691-7.
8. Koldewey P et al. (2016). Forces Driving Chaperone Action. Cell 166(2):369-79.
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University of Michigan
Department of Molecular, Cellular, and Developmental Biology
Natural Science Building, Room 4007A
830 N. University
Ann Arbor, MI 48109
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Über University of Michigan
The MCDB department at the University of Michigan consits of thirty-two faculty and over sixty Ph.D. students whose charge is to increase knowledge of living organisms. To do this we focus on basic research at the molecular and cellular levels of all branches of life - bacteria, plants, and animals. Recent advances in the molecular biosciences have led to an explosion of knowledge, providing a...Mehr über die University of Michigan