Biological Physics

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Dr. Donghua H. Zhou Associate Professor Department of Physics Oklahoma State University 230 L Henry Bellmon Research Center Stillwater, OK 74078 (405) 744-3277 (Tel) (405) 744-6811 (Fax) donghua@okstate.edu Lab: 210 G HBRC, 744-2865 Postdoc Chemistry, University of Illinois at Urbana-Champaign 2003-2008 Ph.D. Physics, the College of William and Mary 2003 B.S. Physics, Peking University 1997

Our NMR determined structure of the DNA binding domain of Hop2 (homologous pairing protein 2), which is important to gene diversity when sperms and eggs are produced. Click the figure to show video on its interaction with DNA.

Structure model of Lsd1 (lipid storage droplet protein) to explain membrane anchoring and lipolysis mechanisms.

Model for bone mineral platelet that permitted estimation of specific surface area from NMR measured concentration of structural water.

Research Overview

Our biological physics research focuses on proteins important to health. We use both solution and solid state NMR experimental techniques to study the structure and dynamics of soluble, aggregated, and membrane proteins. Atomic resolution three-dimensional structures of proteins are critical to understand their biological functions and molecular mechanisms of diseases. We also use supercomputer based molecular docking and molecular dynamics (MD) simulation methods to study interactions of potential drug candidates with target proteins, providing important insights on how to redesign molecules for more potent drugs with less side effects.


Team Precision Fermentation
Donghua Zhou, Maria Figueroa (Qualisud, Univ Montpellier, France), Sujan Timsina, Masrur Akhter, Claudia Figueroa (CONACYT-Tecnológico Nacional de México, Mexico), Patricia Rayas-Duarte (Robert M. Kerr Food & Agricultural Products Center)

Publications (pubmed)

(* as corresponding author; ^† member in Zhou group)

(30) "Reconstitution and resonance assignments of yeast OST subunit Ost4 and its critical mutant Ost4V23D in liposomes by solid-state NMR", Chaudhary; B. P, Struppe, J.; Moktan, H.^†; Zoetewey, D.; Zhou, D. H.; Mohanty, S. J. Biomol. NMR, 2024, ___, ___. (Published online February 29, 2024).

(29) "The advance of anti-cancer flexible heteroarotinoids compounds", Mashayekhi, M.^†; Zhou, D. H., J. Biochem. Mol. Biol. Res., 2020, 5, 230-241. (Published online July 28, 2020).

(28) "Tetrahydroquinoline units in flexible heteroarotinoids (Flex-­Hets) convey anti-­cancer properties in A2780 ovarian cancer cells", Gnanasekaran, K. K.; Pouland, T; Bunce, R. A.; Berlin, K. D.; Abuskhuna, S.; Bhandari, D.^†; Mashayekhi, M.^†; Zhou, D. H.; Benbrook, D. M., Bioorg. Med. Chem., 2020, 28, 115244. ( Published online December 2, 2019).

(27) "Subcellular Organelles: Lipid Droplets and the Multifunctional Roles", Lin, P.; Zhou, D. H.*, Chapter 7 in The Molecular Nutrition of Fats, Patel, V. (ed), Acacemic Press (an imprint of Elsevier), 2018, 87-101. (Release date Nov. 9, 2018 Note: listed as Chapter 24 in this preliminary TOC).

(26) "Novel activity of oxygen- versus sulfur-containing analogs of the flex-het anticancer agent SHetA2", Watts, F., Jr.; Pouland, T.; Bunce, R. A.*; Berlin, K. D.; Benbrook, D. M.*; Mashayekhi, M.^†; Bhandari, D.^†; Zhou, D. H.*, European J. Med. Chem., 2018, 158, 720-732. (Published online September 14, 2018).

(25) "Wing 1 of protein HOP2 is as important as helix 3 in DNA binding by MD simulation", Moktan, H.^†; Zhou, D. H.*; J. Biomol. Struct. Dyn., 2018, 36, 1853-1866. (Published online Jun 8, 2017).

(24) "Solution structure and DNA-binding properties of the winged helix domain of the meiotic recombination HOP2 protein", Moktan, H.^†; Guiraldelli, M. F. ; Eyter, C. A.; Zhao, W.; Lee, C.-Y.; Camerini-Otero, R. D.; Sung, P.; Zhou, D. H.^†; Pezza, R. J.; J. Biol. Chem., 2014, 289, 14682-14691. (Published online April 7, 2014).

(23) "Membrane attachment and structure models of lipid storage droplet protein 1", Lin, P. H.^†; Chen, X.; Moktan, H.^†; Arrese, E. L.; Duan, L.^†; Wang, L. Y.^†; Soulages, J. L.; Zhou, D. H.*; BBA-Biomembranes, 2014, 1838, 874-881. (Published online, Dec. 13, 2013).

(22) "Analyses of mineral specific surface area and hydroxyl substitution for intact bone", Taylor, A. J.^†; Rendina E.; Smith, B. J.; Zhou, D. H.*; Chem. Phys. Lett., 2013, 588, 124-130. (Published online, October 5, 2013).

(21) "High-resolution proton CRAMPS NMR using narrowband analog filters and postponed data acquisition", Wang, L. Y.^†; Zhou, D. H.*; J. Magn. Reson., 2013, 234, 141-146. (Published online, Jul. 1, 2013).

(20) "Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy", Zhou, D. H.*; Nieuwkoop, A. J.; Berthold, D. A.; Comellas, G.; Sperling, L. J.; Tang, M.; Shah, G. J.; Brea, E. J.; Lemkau, L. R.; Rienstra, C. M., J. Biomol. NMR 2012, 54, 291-305. (Published online, September 20, 2012).

(19) "Structural intermediates during alpha-synuclein fibrillogenesis on phospholipid vesicles", Comellas G.; Lemkau L.R.; Zhou, D.H.; George J.M.; Rienstra, C.M. J. Am. Chem. Soc., 2012, 134, 5090-5099. ( Published online, February 21, 2012).

(18) “Fast magic angle spinning for protein solid-state NMR spectroscopy”, Zhou, D. H.*, Chapter 18 in Solid-State NMR Studies of Biopolymers, McDermott, A.E. and Polenova, T. (eds), John Wiley & Sons, Ltd., Chichester, UK, 2010, 331-342.

(17) “Fast magic angle spinning for protein solid-state NMR spectroscopy”, Zhou, D. H.*, Encyclopedia Magn. Reson. McDermott, A.E. and Polenova, T. (section eds), Harris, R. K. and Wasylishen, R. E. (eds), John Wiley & Sons, Ltd., Chichester, UK, 2010. (Published online, March 15, 2010).

(16) “Proton-detected solid-state NMR of natural abundance peptide and protein pharmaceuticals”, Zhou, D. H.; Shah, G.; Mullen, C.; Sandoz, D.; Rienstra, C. M., Angew. Chem. Int. Ed. 2009, 48, 1253-1256. (Published online, January 7, 2009).

Recommended by Faculty of 1000 Biology, March 25, 2009.

(15) “Rapid analysis of organic compounds by proton-detected fast-MAS heteronuclear correlation NMR spectroscopy”, Zhou, D. H.; Rienstra, C. M., Angew. Chem. Int. Ed. 2008, 47, 7328-7331. (Published online, August 6, 2008).

(14) “High-performance solvent suppression for high-sensitivity biomolecular solid-state NMR”, Zhou, D. H.; Rienstra, C. M., J. Magn. Reson. (Communication) 2008, 192, 167-172. (Published online, February 1, 2008).

(13) “Conformation-specific binding of alpha-synuclein to novel protein partners detected by phage display and NMR spectroscopy”, Woods, W. S.; Boettcher, J. M.; Zhou, D. H.; Kloepper, K. D.; Hartman, K. L.; Ladror, D. T.; Qi, Z.; Rienstra, C. M.; George, J. M. J. Biol. Chem. 2007, 282, 34555-34567. (Published online, Sep. 25, 2007).

(12) “Solid-state protein structure determination with proton-detected triple resonance 3D magic-angle spinning NMR spectroscopy”, Zhou, D. H.; Shea, J. J.; Nieuwkoop, A. J.; Franks, W. T.; Wylie, B. J.; Mullen, C.; Sandoz, D.; Rienstra, C. M., Angew. Chem. Int. Ed. 2007, 46, 8380-8383. (Published online, Oct. 1, 2007).

(11) “Proton-detected solid-state NMR spectroscopy of fully protonated proteins at 40 kHz magic-angle spinning”, Zhou, D. H.; Shah, G.; Cormos, M.; Mullen, C.; Sandoz, D.; Rienstra, C. M., J. Am. Chem. Soc. 2007, 129, 11791-11801. (Published online August 29, 2007).

Featured in the May 2008 issue of Chemistry World, Royal Society of Chemistry, Snapshots from the NMR frontier (Ref#1)

Selected as Must Read by Faculty of 1000 Biology, Dec. 19, 2007

More information about Varian FastMAS^TM probes

(10) “Temperature-dependent sensitivity enhancement of solid-state NMR spectra of alpha-synuclein fibrils”, Kloepper, K. D.; Zhou, D. H.; Li, Y.; Winter, K. A.; George, J. M.; Rienstra, C. M., J. Biomol. NMR. 2007, 39, 197-211. (Published online, September 28, 2007.).

(9) “Magic-angle spinning solid-state NMR of a 144 kDa membrane protein complex: E. coli cytochrome bo₃ oxidase”, Frericks, H. L.; Zhou, D. H.; Yap, L.; Gennis, R. B.; Rienstra, C. M., J. Biomol. NMR. 2006, 36, 55-71. (Published online, Sep. 9, 2006).

(8) “Constant-time through-bond ¹³C correlation spectroscopy for assigning protein resonances with solid-state NMR spectroscopy”, Chen, L.; Olsen, R. A.; Elliot, D. W.; Boettcher, J. M.; Zhou, D. H.; Rienstra, C. M.; Mueller, L. J.; J. Am. Chem. Soc. (Communication) 2006, 128, 9992-9993. (Published online, July 19, 2006).

(7) “Band-selective ¹³C homonuclear 3D spectroscopy for solid proteins at high field with rotor-synchronized soft pulses”, Zhou, D. H.; Kloepper, K. D.; Winter, K. A.; Rienstra, C. M., J. Biomol. NMR 2006, 34, 245-257. (Published online, February 10, 2006).

(6) “Sensitivity and resolution in proton solid-state NMR at intermediate deuteration levels: Quantitative line width analysis and applications to correlation spectroscopy”, Zhou, D. H.; Graesser, D. T.; Franks, W. T.; Rienstra, C. M., J. Magn. Reson. 2006, 178, 297-307. (Published online, November 10, 2005).

(5) “Magic-angle spinning solid-state NMR spectroscopy of the ß1 immunoglobulin binding domain of protein G (GB1): ¹⁵N and ¹³C chemical shift assignments and conformational analysis”, Franks, W. T.; Zhou, D. H.; Wylie, B. J.; Money, B. G.; Graesser, D. T.; Frericks, H. J.; Sahota, G.; Rienstra, C. M., J. Am. Chem. Soc. 2005 127, 12291-12305. (Published online August 11, 2005).

(4) “Reduction of RF-induced sample heating with a scroll coil resonator structure for solid-state NMR probes”, Stringer, J. S; Bronnimann, C. E.; Mullen, C. G.; Zhou, D. H.; Stellfox, S. A.; Li, Y.; Williams, E. H.; Rienstra, C.M. J. Magn. Reson. (Cover Article; first among UIUC contributors) 2005, 173, 40-48. (Published online December 15, 2004).

More BioMAS probe information at Varian.