Group News

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

vladizha@ uoguelph.ca

December 10: Andrew Gravelle has defended his M. Sc. Thesis

September 10: Emily Ritz has joined the group as a new M. Sc. student.

December 09: Lichi Shi has defended his PhD. Thesis

August 09: Mumdooh Ahmed has defended his PhD. Thesis

July 09: Meaghan Ward has joined the group as a new M. Sc. student.

Teaching Links

Recent publications

2011

  1. M.E. Ward, L. Shi, E.M. Lake, S.Krishnamurthy,H. Hutchins, L.S. Brown, V. Ladizhansky, 2001. "Proton Detected Solid-State NMR Reveals Intramembrane Polar Networks in a Seven-Helical Transmembrane Protein Proteorhodopsin". J. Am. Chem. Soc., in press.
  2. 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.
  3. 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.
  4. 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 .
  5. 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.

    2010

    1. 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.
    2. R. Janik, E. Ritz, A. Gravelle, L. Shi, X. Peng, V. Ladizhansky, 2010. "Interresidue carbonyl-carbonyl polarization transfer experiments in uniformly 13C,15N- labeled peptides and proteins". J. Magn. Reson., 203, 177-184.
    3. D. S. Libich, M. A.M. Ahmed, L. Zhong, V. V. Bamm, V. Ladizhansky, and G. Harauz, 2010. "Fuzzy complexes of myelin basic protein - NMR investigations of a polymorphic organizational linker of the central nervous system". Biochemistry and Cell Biology, 88, 143-155.

    2009

    1. V. Ladizhansky, 2009. "Torsion angle measurements for protein structure determination" in press. In T. Polenova and A.E. McDermott (editors), "Encyclopedia of Magnetic Resonance" (NMR in Biochemistry and Biophysics) and a "Handbook on Biopolymers" (edited by R. E. Wasylishen and R. K. Harris). John Wiley & Sons, Ltd.
    2. 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.
    3. V. Ladizhansky, 2009. Homonuclear dipolar recoupling techniques for structure determination in uniformly 13C-labeled proteins. Solid State Nucl. Magn. Reson., 36, 119-28.
    4. G. Harauz, V. Ladizhansky, J.M. Boggs, 2009. "Structural polymorphism and multifunctionality of myelin basic protein", Biochemistry, 48, 8094-8104.
    5. M. Aluas, C. Tripon, J.M. Griffin, X. Filip, V. Ladizhansky, R.G. Griffin, S.P. Brown, and C. Filip, 2009. "CHHC and 1H-1H magnetization exchange: analysis by experimental solid-state NMR and 11-spin density-matrix simulations". J. Magn. Reson., 199, 1173-1187.
    6. 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.
    7. 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.

    2008

    1. 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.
    2. 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.
    3. 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.

    2007

    1. 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.
    2. R. Janik, X. Peng, and V. Ladizhansky, 2007. 13C-13C distance measurements in U-13C, 15N-labeled peptides using rotational resonance width experiment with a homogeneously broadened matching condition," J. Magn. Reson., 188, 129-140.
    3. M. Ahmed, V. Bamm, G. Harauz, and V. Ladizhansky, 2007. "The BG21 isoform of Golli myelin basic protein is intrinsically disordered with a highly flexible amino-terminal domain," Biochemistry, 46, 9700-9712.
    4. V. Bamm, M. Ahmed, V. Ladizhansky, and G. Harauz, 2007. "Purification and spectroscopic characterization of the recombinant BG21 isoform of murine Golli myelin basic protein", J. Neurosci. Res., 85, 272-284.