We are looking to fill postdoctoral positions in my lab. See below.
Postdoctoral positions in the Barondeau lab at Texas A&M University Department of Chemistry are available immediately for highly motivated, creative individuals with a strong interest in biophysical and/or bioinorganic chemistry. Our labs are located in the Interdisciplinary Life Sciences building (http://vpr.tamu.edu/resources/ilsb), where we have access to state-of-the-art facilities for structural biology, mass spectrometry, and enzymology.
Our group is focused on understanding metallocofactor assembly and the functional tuning partnership between metallocofactors and their protein environments.
Project 1. Structure-function studies of the human Fe-S assembly complex. This project combines recombinant DNA methods with enzymology, chemical biology, and structural methods and is funded by the NIH (renewed in 2017). We recently reported crystal and EM structures along with functional properties of the mitochondrial cysteine desulfurase (NFS1-ISD11-ACP) complex (https://www.ncbi.nlm.nih.gov/pubmed/28634302).
Highlights of our study:
We report lock-and-key or anchoring interactions between the acyl-chain of ACP and ISD11 (a member of the eukaryotic-specific LYRM protein superfamily) along with a novel cysteine desulfurase architecture. This core cysteine desulfurase complex also binds three additional proteins, including the Friedreich’s ataxia protein frataxin, to generate the fully functional Fe-S cluster assembly complex. Our objectives are to elucidate structural properties for how these additional proteins bind to the core complex and provide mechanistic details of how allosteric protein interactions, lipid binding, and post-translational modifications modulate Fe-S cluster biosynthesis.
Project 2. Fluorophore labeling and kinetic interrogation of Fe-S assembly pathways. This project (funded by the NSF) combines chemical biology, fluorescent plate reader and circular dichroism based assays and global fit kinetic analysis to elucidate the function of proteins in bacterial Fe-S assembly and transfer pathways. We have previously reported an intein-based approach to fluorophore label Fe-S proteins with rhodamine and then use fluorescence to monitor cluster content. This approach has the advantage of only monitoring Fe-S clusters bound to the protein or protein complex that is labeled with the fluorophore. For additional information see http://pubs.acs.org/doi/10.1021/ja510998s and http://pubs.acs.org/doi/abs/10.1021/acschembio.6b00632. Our objectives are to test the proposed roles of iron donor, activator/inhibitor, chaperone, intermediate carrier and cluster conversion proteins as well as evaluate kinetic vs thermodynamic control in transfer and regulatory pathways.
Contact Dr. David Barondeau (firstname.lastname@example.org) for additional details.
To apply for a position, please submit a brief description of research interests, career goals, CV, and contact information for three references.
David P. Barondeau
Department of Chemistry
Texas A&M University
301 Old College Main
College Station, TX 77843
Office: ILSB 1196A
Phone: (979) 458-0735