On behalf of Dr Marius Clore: 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 mari...@intra.niddk.nih.gov 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. This email and any attachments are intended solely for the use of the named recipients. If you are not the intended recipient you must not use, disclose, copy or distribute this email or any of its attachments and should notify the sender immediately and delete this email from your system. UK Research and Innovation (UKRI) has taken every reasonable precaution to minimise risk of this email or any attachments containing viruses or malware but the recipient should carry out its own virus and malware checks before opening the attachments. UKRI does not accept any liability for any losses or damages which the recipient may sustain due to presence of any viruses. ######################################################################## To unsubscribe from the CCP4BB list, click the following link: https://www.jiscmail.ac.uk/cgi-bin/WA-JISC.exe?SUBED1=CCP4BB&A=1 This message was issued to members of www.jiscmail.ac.uk/CCP4BB, a mailing list hosted by www.jiscmail.ac.uk, terms & conditions are available at https://www.jiscmail.ac.uk/policyandsecurity/
