doi.bio/hassane_s_mchaourab


Hassane S. Mchaourab, PhD

Early Life and Education

Hassane S. Mchaourab was born in Beirut, Lebanon, and attended the American University of Beirut, where he majored in Physics and pursued a Master's degree. Due to the civil war, he did not complete his Master's and instead moved to the United States, where he obtained his PhD in Biophysics from the Medical College of Wisconsin under the supervision of James S. Hyde. His PhD thesis focused on the development of the theory and instrumentation of EPR spectroscopy.

Career and Research

Mchaourab is currently a Professor of Molecular Physiology & Biophysics, Professor of Physics & Chemistry, and the Louise B. McGavock Chair at the Vanderbilt University School of Medicine. He also has appointments at the Vanderbilt University Center for Structural Biology and the Vanderbilt SOM Quantitative & Chemical Biology Program.

Previously, he completed postdoctoral research at the Jules Stein Eye Institute, UCLA, in the laboratory of Wayne L. Hubbell, where he applied EPR spectroscopy to understanding protein dynamics. This has been the main theme of his research since he started his own lab in 1997.

The Mchaourab laboratory develops and applies spectroscopic methods, including EPR and fluorescence, to understand the dynamic dimension of protein structures. The lab has a particular focus on active transport, with the goal of mapping the conformational motion that couples energy input to transport. Their targets include ABC transporters (MsbA), the Small multidrug resistance transporter (EmrE), and bacterial homologs of neurotransmitter transporters (LeuT).

Notable Works

Google Scholar

HASSANE S MCHAOURAB

Vanderbilt University

https://lab.vanderbilt.edu/mchaourab-lab/

Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics HS Mchaourab, MA Lietzow, K Hideg, WL Hubbell Biochemistry 35 (24), 7692-7704, 1996 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:u5HHmVD_uO8C

Watching proteins move using site-directed spin labeling WL Hubbell, HS Mchaourab, C Altenbach, MA Lietzow Structure 4 (7), 779-783, 1996 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:u-x6o8ySG0sC

Molecular architecture of human prion protein amyloid: A parallel, in-register β-structure NJ Cobb, FD Sönnichsen, H Mchaourab, WK Surewicz Proceedings of the National Academy of Sciences 104 (48), 18946-18951, 2007 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:UeHWp8X0CEIC

Protein structure determination using long-distance constraints from double-quantum coherence ESR: study of T4 lysozyme PP Borbat, HS Mchaourab, JH Freed Journal of the American Chemical Society 124 (19), 5304-5314, 2002 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:qjMakFHDy7sC

Subunit exchange of small heat shock proteins: analysis of oligomer formation of αA-crystallin and Hsp27 by fluorescence resonance energy transfer and site-directed truncations MP Bova, HS Mchaourab, Y Han, BKK Fung Journal of Biological Chemistry 275 (2), 1035-1042, 2000 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:d1gkVwhDpl0C

Structure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins HS Mchaourab, JA Godar, PL Stewart Biochemistry 48 (18), 3828-3837, 2009 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:8k81kl-MbHgC

Conformation of T4 lysozyme in solution. Hinge-bending motion and the substrate-induced conformational transition studied by site-directed spin labeling HS Mchaourab, KJ Oh, CJ Fang, WL Hubbell Biochemistry 36 (2), 307-316, 1997 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:2osOgNQ5qMEC

Toward the fourth dimension of membrane protein structure: insight into dynamics from spin-labeling EPR spectroscopy HS McHaourab, PR Steed, K Kazmier Structure 19 (11), 1549-1561, 2011 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:blknAaTinKkC

Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies DA Haley, MP Bova, QL Huang, HS Mchaourab, PL Stewart Journal of molecular biology 298 (2), 261-272, 2000 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:9yKSN-GCB0IC

Mechanism of NMDA receptor channel block by MK-801 and memantine X Song, MØ Jensen, V Jogini, RA Stein, CH Lee, HS Mchaourab, … Biophysical Journal 114 (3), 24a-25a, 2018 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:Z5m8FVwuT1cC

De novo mutation in the dopamine transporter gene associates dopamine dysfunction with autism spectrum disorder PJ Hamilton, NG Campbell, S Sharma, K Erreger, F Herborg Hansen, … Molecular psychiatry 18 (12), 1315-1323, 2013 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:B3FOqHPlNUQC

Sampling alternative conformational states of transporters and receptors with AlphaFold2 D Del Alamo, D Sala, HS Mchaourab, J Meiler Elife 11, e75751, 2022 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:4hFrxpcac9AC

Mechanism of NMDA receptor inhibition and activation S Zhu, RA Stein, C Yoshioka, CH Lee, A Goehring, HS Mchaourab, … Cell 165 (3), 704-714, 2016 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:ZfRJV9d4-WMC

Structure and dynamics of AMPA receptor GluA2 in resting, pre-open, and desensitized states KL Dürr, L Chen, RA Stein, R De Zorzi, IM Folea, T Walz, HS Mchaourab, … Cell 158 (4), 778-792, 2014 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:eflP2zaiRacC

Energy transduction and alternating access of the mammalian ABC transporter P-glycoprotein B Verhalen, R Dastvan, S Thangapandian, Y Peskova, HA Koteiche, … Nature 543 (7647), 738-741, 2017 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:z_wVstp3MssC

Mechanism of chaperone function in small heat shock proteins: dissociation of the HSP27 oligomer is required for recognition and binding of destabilized T4 lysozyme R Shashidharamurthy, HA Koteiche, J Dong, HS Mchaourab Journal of Biological Chemistry 280 (7), 5281-5289, 2005 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:eQOLeE2rZwMC

Structural basis of energy transduction in the transport cycle of MsbA J Dong, G Yang, HS Mchaourab Science 308 (5724), 1023-1028, 2005 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:Y0pCki6q_DkC

Ion/substrate-dependent conformational dynamics of a bacterial homolog of neurotransmitter: sodium symporters DP Claxton, M Quick, L Shi, FD De Carvalho, H Weinstein, JA Javitch, … Nature structural & molecular biology 17 (7), 822-829, 2010 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:HDshCWvjkbEC

The growing world of small heat shock proteins: from structure to functions S Carra, S Alberti, PA Arrigo, JL Benesch, IJ Benjamin, W Boelens, … Cell Stress and Chaperones 22 (4), 601-611, 2017 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:t7zJ5fGR-2UC

Conformational motion of the ABC transporter MsbA induced by ATP hydrolysis PP Borbat, K Surendhran, M Bortolus, P Zou, JH Freed, HS Mchaourab PLoS biology 5 (10), e271, 2007 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=0OnISMAAAAJ&citationforview=0OnISMAAAAJ:roLk4NBRz8UC










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