Research Description: A NIH-funded postdoctoral position is available immediately to study the cooperative roles and molecular mechanisms of the GTPase dynamin and BAR domain-containing protein partners in synaptic vesicle endocytosis and recycling. The position requires a Ph.D. in an area relevant to cell biology, protein biochemistry or biophysics. The Ramachandran laboratory employs a host of cutting-edge spectroscopic and microscopic approaches including FRET, fluorescence correlation spectroscopy (FCS) and fluorescence lifetime imaging (FLIM) to determine protein-protein and protein-membrane interactions in membrane remodeling and fission both in vitro and in vivo. A working knowledge of fluorescence spectroscopic and imaging techniques, including confocal and TIRF microscopy, is essential. Demonstrated experience in working with model membrane systems such as liposomes and giant unilamellar vesicles (GUVs) and/or the application of FCS and FLIM to assess protein-protein and protein-membrane interactions is desirable. Our laboratory is equipped with state-of-the-art instrumentation for both ensemble and single-molecule level fluorescence spectroscopic/microscopic studies as well as for protein purification, characterization and membrane reconstitution.
Requirements: Applicants must be highly motivated and must have demonstrated experience (i.e. relevant publications) in protein biochemistry, fluorescence spectroscopy, or microscopy. The candidate should have strong conceptual and experimental background in biochemistry and molecular biology, as well as on the mechanistic dissection of structure-function relationships in proteins; background in cell biology is desirable; he/she should be independent, proactive, hard working and productive; only candidates that have first-author publications (or articles in press) in reputed journals will be considered. Salary will commensurate with experience and will adhere to current NIH guidelines. Ph.D. candidates that are ready to graduate or are within one year of graduation are preferred.
Interested candidates should submit their CV, reprints of selected publications, three reference letters (directly from referees), and a cover letter summarizing their experience, long-term goals, and estimated start date directly to firstname.lastname@example.org.
Ramachandran, R. (2011) Vesicle Scission: Dynamin.
Ramachandran, R., Pucadyil, T.J., Liu, Y.W., Acharya, S., Leonard, M., Lukiyanchuk, V., and Schmid, S.L. (2009) Membrane insertion of the pleckstrin homology domain variable loop 1 is critical for dynamin-catalyzed membrane fission. Mol. Biol. Cell. 20, 4630-4639.
Ramachandran, R., and Schmid, S.L. (2008) Real-time detection reveals that effectors couple dynamin’s GTP-dependent conformational changes to the membrane. EMBO J. 27, 27-37.
Ramachandran, R., Surka, M., Chappie, J. S., Fowler, D. M., Foss, T. R., Song, B. D., and Schmid, S. L. (2007) The dynamin middle domain is critical for tetramerization and higher-order self-assembly. EMBO J. 26, 559-566.
Ramachandran, R., Tweten, R. K., and Johnson, A. E. (2005) The domains of a cholesterol-dependent cytolysin undergo a major FRET-detected rearrangement during pore formation. Proc. Natl. Acad. Sci. 102, 7139-7144.
Ramachandran, R., Tweten, R. K., and Johnson, A. E. (2004) Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit b-strand alignment. Nature Structural & Molecular Biology 11, 697-705.
Ramachandran, R., Heuck, A. P., Tweten, R. K., and Johnson, A. E. (2002) Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin. Nature Structural Biology 9, 823-827.
Case Western Reserve University is an Equal Opportunity Employer encouraging excellence through diversity. Qualified woman and minority candidates are encouraged to apply.
Case Western Reserve University provides reasonable accommodations to applicants with disabilities. Applicants requiring a reasonable accommodation for any part of the application and hiring process should contact the Office of Inclusion, Diversity and Equal Opportunity at 216-368-8877 to request a reasonable accommodation. Determinations as to granting reasonable accommodations for any applicant will be made on a case-by-case basis.