Group News

Our group is looking to expand with positions for M. Sc. and Ph. D. students open. For more information see the projects page or contact Prof. Ladizhansky directly at:

vladizha@ uoguelph.ca

September 6, 2017: David Bolton has defended his M.Sc Thesis

July 23, 2017 : Daryl Good received best poster award at ISMAR 2017

June 30, 2017 : David Park has has defended his M.Sc Thesis

May 2017 : Congratylations to Daryl on his JACS paper

April 20, 2017: Jeffrey De Vlugt has joined the group as an M.Sc student

September 1, 2016: Xiao Peng has joined the group as a Ph.D student

September 1, 2016: Dylan Dingwell has continued as an M.Sc. student

June 30, 2017: Meg Ward has defended her Ph.D. Thesis

Selected publications

V. Ladizhansky, 2017. Applications of solid-state NMR to membrane proteins. DOI: 10.1016/j.bbapap.2017.07.004.

D. Good, C. Pham, J. Jagas, J.R. Lewandowski, V. Ladizhansky, 2017. Solid-State NMR Provides Evidence for Small-Amplitude Slow Domain Motions in a Multispanning Transmembrane α-Helical Protein. J. Am. Chem. Soc., 139, 9246.

S. Milikisiyants, S. Wang, R.A. Munro, M. Donohue, M.E. Ward, D. Bolton, L.S. Brown, T.I. Smirnova, V. Ladizhansky, A.I. Smirnov, 2017. Oligomeric Structure of Anabaena Sensory Rhodopsin in a Lipid Bilayer Environment by Combining Solid-State NMR and Long-range DEER Constraints. J. Mol. Biol., 429, 1903.

S. Wang, C. Ing, S. Emami, Y. Jiang, H. Liang, R. Pomès, L.S. Brown, V. Ladizhansky. 2016. Structure and Dynamics of Extracellular Loops in Human Aquaporin-1 from Solid-State NMR and Molecular Dynamics. J. Phys. Chem. B. 120, 9887.

M.A. Rogers, Q. Feng, V. Ladizhansky, D.B. Good, A.K. Smith, M. Corridini, D.A.S. Grahame, B.C. Bryksa, P.D. Jadhav, S. Sammynaiken, L.-T. Lim, B. Guild, Y.Y. Shim, P.-G. Burnett, M.J.T. Reaney, 2016. Self-assembled fibrillar networks comprised of a naturally-occurring cyclic peptide—LOB3. RSC Advances 6, 40765.

M.E. Ward, E. Ritz, M.A. Ahmed, V.V. Bamm, G. Harauz, L.S. Brown, V. Ladizhansky, 2015. Proton detection for signal enhancement in solid-state NMR experiments on mobile species in membrane proteins. J. Biomol. NMR 63, 375.

M.A. Voinov, D.B. Good, M.E. Ward, S. Milikisiyants, A. Marek, M.A. Caporini, M. Rosay, R.A. Munro, M. Ljumovic, L.S. Brown, V. Ladizhansky, A.I. Smirnov, 2015. Cysteine-Specific Labeling of Proteins with a Nitroxide Biradical for Dynamic Nuclear Polarization NMR. J. Phys. Chem. B. 119, 10180.

L.S. Brown, V. Ladizhansky, 2015. Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy. Prot. Sci. 24, 1333. Editors Highlights

M.E. Ward, S. Wang, R. Munro, E. Ritz, I. Hung, P.L. Gor'kov, Y. Jiang, H. Liang, L.S. Brown, V. Ladizhansky, 2015. In situ structural studies of Anabaena sensory rhodopsin in the E. coli membrane. Biophys J. 108, 1683. Article featured as New and Notable

M.E. Ward, L.S. Brown, V. Ladizhansky, 2015. Advanced solid-state NMR techniques for characterization of membrane protein structure and dynamics: application to Anabaena Sensory Rhodopsin. J. Magn. Reson. 253, 119.

S. Wang,V. Ladizhansky, 2014. Recent advances in magic angle spinning solid state NMR of membrane proteins. Prog. Nucl. Magn. Reson. Spectrosc. 82, 1.

V. Ladizhansky, 2014. Recent advances in magic angle spinning solid-state NMR of proteins. Isr. J. Chem. 54, 866

D.B. Good, S. Wang, M.E. Ward, J. O. Stuppe, L.S. Brown, J. Lewandowski, V. Ladizhansky. 2014. Conformational dynamics of a seven transmembrane helical protein Anabaena Sensory Rhodopsin probed by solid-state NMR. J. Am. Chem. Soc. 36, 2833. Article selected for JACS Spotlights

L. Kuang, D.A. Fernandes, M. O'Halloran, W. Zheng, Y. Jiang, V. Ladizhansky, L.S. Brown, H. Liang, 2014. "Frozen" Block Copolymer Nanomembranes with Light-Driven Proton Pumping Performance.ACS Nano, 28, 537.

M.E.Ward, S. Wang, S. Krishnamurthy, H. Hutchins, M. Fey, L.S. Brown, V. Ladizhansky, 2014. High-resolution paramagnetically enhanced solid-state NMR spectroscopy of membrane proteins at fast magic angle spinning. J. Biomol. NMR, 58, 37.

G.T. Debelouchina, M.J. Bayro, A.W. Fitzpatrick, V. Ladizhansky, M.T. Colvin, M.A. Caporini, C.P. Jaroniec, V.S. Bajaj, M. Rosay, C.E. Macphee,M. Vendruscolo, W.E. Maas, C.M. Dobson, R.G. Griffin, 2013 .Higher Order Amyloid Fibril Structure by MAS NMR and DNP Spectroscopy. J. Am. Chem. Soc, 135, 19237.

S. Wang, R.A. Munro, L. Shi, I. Kawamura, T. Okitsu, A. Wada, S.Y. Kim, K.H. Jung, L.S. Brown, V. Ladizhansky, 2013. Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein. Nature Methods, 10, 1007.

A.W. Fitzpatrick, G.T. Debelouchina, M.J. Bayro, D.K. Clare, M.A. Caporini, V.S. Bajaj, C.P. Jaroniec, L. Wang, V. Ladizhansky, S.A. MN|ller, C.E. MacPhee, C.A. Waudby, H.R. Mott, A. De Simone,T.P. Knowles, H.R. Saibil,M. Vendruscolo, E.V. Orlova, R.G. Griffin, C.M. Dobson, 2013. Atomic structure and hierarchical assembly of a cross-beta amyloid fibril. Proc Natl Acad Sci U S A., 110, 5468.

S. Emami, Y. Fan, R. Munro, V. Ladizhansky, L.S. Brown, 2013. Yeast-expressed human membrane protein aquaporin-1 yields excellent resolution of solid-state MAS NMR spectra. J Biomol NMR. 55, 147.

S. Wang, R.A. Munro, S.Y. Kim, K.H. Jung, L.S. Brown, V. Ladizhansky, 2012. Paramagnetic relaxation enhancement reveals oligomerization interface of a membrane protein. J Am Chem Soc. 2012, 134, 16995.

S. Wang, L. Shi, T. Okitsu, A. Wada, L.S. Brown, V. Ladizhansky, 2013. Solid-state NMR (13)C and (15)N resonance assignments of a seven-transmembrane helical protein Anabaena Sensory Rhodopsin. Biomol NMR Assign, 7, 253.

L. Shi, V. Ladizhansky, 2012. Magic angle spinning solid-state NMR experiments for structural characterization of proteins. Methods Mol Biol. 895, 153.

M.E. Ward, L. Shi, E.M. Lake, S.Krishnamurthy,H. Hutchins, L.S. Brown, V. Ladizhansky, 2011. Proton Detected Solid-State NMR Reveals Intramembrane Polar Networks in a Seven-Helical Transmembrane Protein Proteorhodopsin. J. Am. Chem. Soc., 133, 17434-17443

S. Wang, L. Shi, I. Kawamura, L.S. Brown, V. Ladizhansky, 2011. Site-Specific Solid-State NMR Detection of Hydrogen-Deuterium Exchange Reveals Conformational Changes in a 7-Helical Transmembrane Protein. Biophys. J, 101, L23-L25.

S. Wang, S.Y. Kim, K.-H. Jung, V. Ladizhansky, L.S. Brown, 2011. A Eukaryotic-Like Interaction of Suluble Cyanobacterial Sensory Rhodopsin Transducer with DNA. J. Mol. Biol., 411, 449-462.

L. Shi, I. Kawamura, K.-H. Jung, L. S. Brown, V. Ladizhansky, 2011. Molecular conformation of a seven-helical transmembrane photosensor in the lipid environment. Angew. Chemie Int. Ed., 50, 1302-1305 .

Y. Fan, L. Shi, V. Ladizhansky, L.S. Brown, 2011. Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment. J Biomol NMR, 49, 151-161.

M.A. Ahmed, V.V. Bamm, G. Harauz, V. Ladizhansky, 2010. Solid-state NMR spectroscopy of membrane-associated myelin basic protein-conformation and dynamics of an immunodominant epitope, Biophys J. 99, 1247-1255.

L. Shi, E. Lake, M. Ahmed, L.S. Brown and V. Ladizhansky, 2009. Solid-state NMR study of proteorhodopsin in the lipid environment: secondary structure and dynamics. BBA-Biomembranes, 1788, 2563-2574

V. Ladizhansky, 2009. Homonuclear dipolar recoupling techniques for structure determination in uniformly 13C-labeled proteins. Solid State Nucl. Magn. Reson., 36, 119-28.

L. Shi, M. A. Ahmed, G. Whited, W. Zhang, L. S. Brown, V. Ladizhansky, 2009. "Three-dimensional solid-state NMR study of seven-helical integral membrane proton pump: partial spectral assignments and structural insights", J. Mol. Biol. 386, 1078-1093.

M. A. Ahmed, V. V. Bamm, L. Shi, M. Steiner-Mosonyi, J. F. Dawson, L.S. Brown, G. Harauz, V. Ladizhansky, 2009. "Induced secondary structure and polymorphism in an intrinsically disordered structural linker of the CNS - Solid-state NMR and FTIR spectroscopy of 18.5 kDa myelin basic protein bound to actin", Biophys. J., 96, 180-191.

L. Shi, X. Peng, M.A. Ahmed, D. Edwards, L.S. Brown, V. Ladizhansky, 2008. "Resolution enhancement by homonuclear J-decoupling: application to three-dimensional solid-state magic angle spinning NMR spectroscopy". J Biomol. NMR, 41, 9-15.

X. Peng, D. Libich, R. Janik, G. Harauz, and V. Ladizhansky, 2008. "Dipolar Chemical Shift Correlation Spectroscopy for Homonuclear Carbon Distance Measurements in Proteins in the Solid State: Application to Structure Determination and Refinement", J. Am. Chem. Soc., 130, 359-369.

G. Harauz, V. Ladizhansky, 2008. "Structure and dynamics of the myelin basic protein (MBP) family by solution and solid-state NMR". Chapter X (pp 196-231) in Joan M. Boggs (editor),"Myelin Basic Protein", Series on "Intrinsically Disordered Proteins" (edited by Vladimir Uversky). Nova Science Publishers.

L. Zhong, V. Bamm, M.A. Ahmed, G. Harauz, and V. Ladizhansky, 2007. "Solid-state NMR spectroscopy of 18.5 kDa myelin basic protein reconstituted with lipid vesicles: spectroscopic characterisation and spectral assignments of solvent-exposed protein fragments", BBA-Biomembranes, 1768, 3193-3205.