Dear Friends and Colleagues,
Positions are now available for training in my lab at the undergraduate, Masters, PhD and Postdoc levels to study protein folding in vivo. If you know of someone that may be interested please forward this email to him or her. Funding is available.
Our lab directs evolution to improve protein folding. We aim to understand protein folding well enough to be able to manipulate it in vivo. We ask organisms themselves to solve difficult protein folding problems and by examining their solutions we can better understand folding in the cell. We have developed folding biosensors that link protein stability to antibiotic resistance that enables us to optimize folding in vivo (1) and discover new molecular chaperones (2). We are stabilizing disease related proteins including the HIV tail spike protein
with the hope of generating an effective AIDS vaccine. In vivo protein folding is intimately tied to the action of folding catalysts and chaperones. We study the action of these folding helpers both in vivo and in vitro using a wide range of genetic, biochemical, biophysical and structural techniques(3).
If you know of someone that is interested please have them send me a resume that includes your contact information, a description of your research experience, names email addresses and phone numbers of 3 people who can serve as references and a list of the grades that they have received in classes. Ann Arbor provides a great scientific and cultural 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. Epub Feb 13, 2011.
3. Tapley T et. al. (2010) Protein refolding by pH-triggered chaperone binding and release. Proc Natl Acad Sci U S A 107: 1071-1076.
Please feel free to pass this on to whomever you think may be interested. I would also appreciate it if you could post this flier (http://www.mcdb.lsa.umich.
Positions are now available for training in my lab at the undergraduate, Masters, PhD and Postdoc levels to study protein folding in vivo. If you know of someone that may be interested please forward this email to him or her. Funding is available.
Our lab directs evolution to improve protein folding. We aim to understand protein folding well enough to be able to manipulate it in vivo. We ask organisms themselves to solve difficult protein folding problems and by examining their solutions we can better understand folding in the cell. We have developed folding biosensors that link protein stability to antibiotic resistance that enables us to optimize folding in vivo (1) and discover new molecular chaperones (2). We are stabilizing disease related proteins including the HIV tail spike protein
with the hope of generating an effective AIDS vaccine. In vivo protein folding is intimately tied to the action of folding catalysts and chaperones. We study the action of these folding helpers both in vivo and in vitro using a wide range of genetic, biochemical, biophysical and structural techniques(3).
If you know of someone that is interested please have them send me a resume that includes your contact information, a description of your research experience, names email addresses and phone numbers of 3 people who can serve as references and a list of the grades that they have received in classes. Ann Arbor provides a great scientific and cultural 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. Epub Feb 13, 2011.
3. Tapley T et. al. (2010) Protein refolding by pH-triggered chaperone binding and release. Proc Natl Acad Sci U S A 107: 1071-1076.
Please feel free to pass this on to whomever you think may be interested. I would also appreciate it if you could post this flier (http://www.mcdb.lsa.umich.
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