A postdoctoral position is available in the lab of Marius Clore in the Laboratory of Chemical Physics at the National Institutes of Health in Bethesda, Maryland.
Particular emphasis within the lab concerns the study of excited states involved in molecular recognition and fibril assembly using state-of-the-art NMR and EPR spectroscopy. Current focus is on the study of the mechanism of aggregation of huntingtin and the study of various chaperones with anti-aggregation and disaggregation properties. Additional work is also being carried out using time resolved DEER EPR and solid state NMR in combination with sub-millisecond freeze quenching to probe complex transient kinetic pathways involved in molecular recognition.
Some recent papers are listed below.
Applicants should e-mail their interest directly to firstname.lastname@example.org include their CV/bibliography and the names of two references.
Recent papers from the lab of Marius Clore:
Kotler, S.A, Tugarinov, V., Schmidt, T., Ceccon, A., Libich, D.S., Ghirlando, R., Schwieters, C.D. and Clore, G.M. (2019) Probing initial transient oligomerization events facilitating Huntingtin fibril nucleation at atomic resolution by relaxation-based NMR. Proc. Natl. Acad. Sci. U. S. A. 116, 3562-3571.
Karamanos, T.K., Tugarinov, V. & Clore, G.M. (2019) Unraveling the structure and dynamics of the human DNAJB6b chaperone by NMR reveals insights into Hsp40-mediated proteostasis. Proc. Natl. Acad. Sci. U.S.A. 116, 21529-21538.
Ceccon, A., Tugarinov, V., Ghirlando, R. & Clore, G.M. (2020) Abrogation of pre-nucleation, transient oligomerization of the Huntingtin exon-1 protein by human profilin-I. Proc. Natl. Acad. Sci. U.S.A. 117, 5844-5852.
Ceccon, A., Tugarinov, V. & Clore, G.M. (2021) Quantitative exchange NMR-based analysis of Huntingtin-SH3 interactions suggests an allosteric mechanism of inhibition of Huntingtin Aggregation. J. Am. Chem. Soc. 143, 9672-9681.
Walti, M.A., Kotler, S.A. & Clore, G.M. (2021) Probing the interacttion of huntingtin exon-1 polypeptides with the chaperonin nanomachine GroEL. ChemBioChem 22, 1985-1991
Okuno, Y., Yoo, J., Schwieters, C.D., Best, R.B., Chung, H.S. & Clore, G.M. (2021) Atomic view of cosolute-induced protein denaturation probed by NMR solvent paramagnetic relaxation enhancement. Proc. Natl. Acad. Sci. U.S.A. 118, e211202118
Schmidt, T., Jeon, J., Yau, W.-M., Schwiters, C.D., Tycko, R. & Clore, G.M. (2022) Time-resolved DEER EPR and solid-state NMR afford kinetic and structural elucidation of substrate binding to Ca2+-ligated calmodulin. Proc. Natl. Acad. Sci. U.S.A. 119, e2122308119.
G. Marius Clore, MD, PhD, DSc (Hon), FRS
NIH Distinguished Investigator
Chief, Section of Molecular and Structural Biophysics
Laboratory of Chemical Physics
Bldg 5/Rm B1-30I
NIDDK, National Institutes of Health
Bethesda, MD 20892-0520
Tel: (301) 496 0782
Fax: (301) 496 0825
web: http://spin.niddk.nih.gov/clore (lab homepage)
http://www.nasonline.org/member-directory/members/20033168.html (National Academy of Sciences web page)
https://royalsociety.org/people/G-Marius-Clore-25341/ (Royal Society web page)
http://www.ae-info.org/ae/Member/Clore_G._Marius (Academia Europaea web page)
https://en.wikipedia.org/wiki/G._Marius_Clore (wikipedia profile)