NMR Publications

Vlad Ladizhansky
George Harauz

Publications from Vlad Ladizhansky

2015

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

  • M.E. Ward, S. Wang, R. Munro, E. Ritz, I. Hung, P. L.Gor�kov, Y. Jiang, H. Liang, L. S. Brown, and V. Ladizhansky , 2015. In Situ Structural Studies of Anabaena Sensory Rhodopsin in the E. coli Membrane Biophys. J., 108, 1683. Highlighted in �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.

2014

  • 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, 86.

  • D.B. Good, S. Wang, M.E. Ward, J. O. Struppe, 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., 136, 2833. Article selected for JACS Spotlights and was featured in the virtual issue on protein dynamics

  • 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, 53 

  • 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. 

2013

  • 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. Mller, 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.

2012

  • 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.

2011

  • 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. (Biophys. Letter), 101, L23.

  • 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. 

  • 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.

2010

  • 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.

  • 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.

  • 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

  • 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.

  • 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.

  • G. Harauz, V. Ladizhansky, J.M. Boggs, 2009. Structural polymorphism and multifunctionality of myelin basic protein, Biochemistry, 48, 8094-8104.

  • M. Aluas, C. Tripon, J.M. Griffin, X. Filip, V. Ladizhansky, R.G. Griffin, S.P. Brown, C. Filip, CHHC and 1H-1H Magnetization Exchange: Analysis by Experimental Solid-State NMR and 11-Spin Density-Matrix Simulations, Journal of Magnetic Resonance 199 (2009) 173-187. http://dx.doi.org/10.1016/j.jmr.2009.04.013

  • L. Shi, M.A.M. Ahmed, W. Zhang, G. Whited, L.S. Brown, V. LadizhanskyThree-dimensional solid-state NMR study of a seven-helical integral membrane proton pump � structural insights, Journal of Molecular Biology 386 (2009) 1078-1093. http://dx.doi.org/10.1016/j.jmb.2009.01.011 

  • M.A.M. Ahmed, V.V. Bamm, L. Shi, M. Steiner-Mosonyi, J.F. Dawson, L. Brown, G. Harauz, V. LadizhanskyInduced Secondary Structure and Polymorphism in an Intrinsically Disordered Structural Linker of the CNS: Solid-State NMR and FTIR Spectroscopy of Myelin Basic Protein Bound to Actin, Biophysical Journal 96 (2009) 180-191. http://dx.doi.org/10.1016/j.bpj.2008.10.003

2008

  • G. Harauz, V. Ladizhansky. 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 V. Uversky). Nova Science Publishers, 2008.

  • L. Shi, X. Peng, M.A.M. Ahmed, D. Edwards, L.S. Brown. and V. Ladizhansky. Resolution enhancement by homonuclear J-decoupling: application to three-dimensional solid-state magic angle spinning NMR spectroscopy. Journal of Biomolecular NMR (2008) in press. http://dx.doi.org/10.1007/s10858-008-9233-7

  • Peng, Xiaohu; Libich, David; Janik, Rafal; Harauz, George; Ladizhansky, Vladimir. Dipolar Chemical Shift Correlation Spectroscopy for Homonuclear Carbon Distance Measurements in Proteins in the Solid State: Application to Structure Determination and Refinement. Journal of the American Chemical Society (2008), 130(1), 359-369.

2007

  • Ahmed, Mumdooh A. M.; Bamm, Vladimir V.; Harauz, George; Ladizhansky, Vladimir. The BG21 Isoform of Golli Myelin Basic Protein Is Intrinsically Disordered with a Highly Flexible Amino-Terminal Domain. Biochemistry (2007), 46(34), 9700-9712.

  • Bamm, Vladimir V.; Ahmed, Mumdooh A. M.; Ladizhansky, Vladimir; Harauz, George. Purification and spectroscopic characterization of the recombinant BG21 isoform of murine golli myelin basic protein. Journal of Neuroscience Research (2007), 85(2), 272-284. 

  • Janik, Rafal; Peng, Xiaohu; Ladizhansky, Vladimir. 13C-13C distance measurements in U-13C, 15N-labeled peptides using rotational resonance width experiment with a homogeneously broadened matching condition. Journal of Magnetic Resonance (2007), 188(1), 129-140. 

  • Zhong, Ligang; Bamm, Vladimir V.; Ahmed, Mumdooh A. M.; Harauz, George; Ladizhansky, Vladimir. 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. Biochimica et Biophysica Acta, Biomembranes (2007), 1768(12), 3193-3205.

2004

  • Ladizhansky, Vladimir; Griffin, Robert G. Band-Selective Carbonyl to Aliphatic Side Chain 13C-13C Distance Measurements in U-13C,15N-Labeled Solid Peptides by Magic Angle Spinning NMR. Journal of the American Chemical Society (2004), 126(3), 948-958.

2003

  • Ladizhansky, Vladimir; Jaroniec, Christopher P.; Diehl, Annette; Oschkinat, Hartmut; Griffin, Robert G. Measurement of Multiple .psi. Torsion Angles in Uniformly 13C,15N-Labeled .alpha.-Spectrin SH3 Domain Using 3D 15N-13C-13C-15N MAS Dipolar-Chemical Shift Correlation Spectroscopy. Journal of the American Chemical Society (2003), 125(22), 6827-6833. 

  • Ladizhansky, V.; Vinogradov, E.; van Rossum, B.-J.; de Groot, H. J. M.; Vega, S. Multiple-spin effects in fast magic angle spinning Lee-Goldburg cross-polarization experiments in uniformly labeled compounds. Journal of Chemical Physics (2003), 118(12), 5547-5557. 

  • Ramachandran, Ramesh; Ladizhansky, Vladimir; Bajaj, Vikram S.; Griffin, Robert G. 13C-13C Rotational Resonance Width Distance Measurements in Uniformly 13C-Labeled Peptides. Journal of the American Chemical Society (2003), 125(50), 15623-15629.

2002

  • Ladizhansky, Vladimir; Veshtort, Mikhail; Griffin, Robert G. NMR determination of the torsion angle .psi. in .alpha.-helical peptides and proteins: the HCCN dipolar correlation experiment. Journal of Magnetic Resonance (2002), 154(2), 317-324.

2000

  • Ladizhansky, V.; Vega, S. Doping of CdS nanoparticles by Co2+ ions studied by NMR. Journal of Physical Chemistry B (2000), 104(22), 5237-5241. 

  • Ladizhansky, Vladimir; Vega, Shimon. Polarization transfer dynamics in Lee-Goldburg cross polarization nuclear magnetic resonance experiments on rotating solids. Journal of Chemical Physics (2000), 112(16), 7158-7168. 

  • Ladizhansky, V.; Hodes, G.; Vega, S. Solid State NMR Study of Water Binding on the Surface of CdS Nanoparticles.Journal of Physical Chemistry B (2000), 104(9), 1939-1943. 

  • Van Rossum, B.-J.; De Groot, C. P.; Ladizhansky, V.; Vega, S.; De Groot, H. J. M. A Method for Measuring Heteronuclear (1H-13C) Distances in High Speed MAS NMR. Journal of the American Chemical Society (2000), 122(14), 3465-3472.

1999

  • Ladizhansky, V.; Lyahovitskaya, V.; Vega, S. 113Cd NMR study of transferred hyperfine interactions in the dilute magnetic semiconductors Cd1-xCoxS and Cd1-xFexS and impurity distribution in Cd0.994Co0.006S. Physical Review B: Condensed Matter and Materials Physics (1999), 60(11), 8097-8104.

1998

  • Ladizhansky, V.; Hodes, G.; Vega, S. Surface Properties of Precipitated CdS Nanoparticles Studied by NMR. Journal of Physical Chemistry B (1998), 102(43), 8505-8509. 

  • Ray, Siddharth; Ladizhansky, Vladimir; Vega, Shimon. Simulation of CPMAS signals at high spinning speeds. Journal of Magnetic Resonance (1998), 135(2), 427-434.

1997

  • Ladizhansky, V.; Faraggi, A.; Lyahovitskaya, V.; Vega, S. NMR study of the diluted magnetic semiconductor alloys Cd1-xMnxSe, Cd1-xCoxSe, and Cd1-xFexSe. Physical Review B: Condensed Matter (1997), 56(11), 6712-6718.

Publications from George Harauz

2009

  • G. Harauz, D.S. Libich. The classic basic protein of myelin - conserved structural motifs and the dynamic molecular barcode involved in membrane adhesion and protein-protein interactions. Current Protein and Peptide Science (Invited Review), 10 (3), pp 196-215, 2009

2008

  • Peng, Xiaohu; Libich, David; Janik, Rafal; Harauz, George; Ladizhansky, Vladimir. Dipolar Chemical Shift Correlation Spectroscopy for Homonuclear Carbon Distance Measurements in Proteins in the Solid State: Application to Structure Determination and Refinement. Journal of the American Chemical Society (2008), 130(1), 359-369.

2007

  • Ahmed, Mumdooh A. M.; Bamm, Vladimir V.; Harauz, George; Ladizhansky, Vladimir. The BG21 Isoform of Golli Myelin Basic Protein Is Intrinsically Disordered with a Highly Flexible Amino-Terminal Domain. Biochemistry (2007), 46(34), 9700-9712.

  • Bamm, Vladimir V.; Ahmed, Mumdooh A. M.; Ladizhansky, Vladimir; Harauz, George. Purification and spectroscopic characterization of the recombinant BG21 isoform of murine golli myelin basic protein. Journal of Neuroscience Research (2007), 85(2), 272-284.

  • Libich, David S; Monette, Martine; Robertson, Valerie J; Harauz, George. NMR assignment of an intrinsically disordered protein under physiological conditions: the 18.5 kDa isoform of murine myelin basic protein. Springer Science+Business Media B.V. (2007), 1:61-63

  • Zhong, Ligang; Bamm, Vladimir V.; Ahmed, Mumdooh A. M.; Harauz, George; Ladizhansky, Vladimir. 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. Biochimica et Biophysica Acta, Biomembranes (2007), 1768(12), 3193-3205.

2006

  • Fare, Christophe; Libich, David S; Harauz, George. Solution NMR structure of an immunodominant epitope of myelin basic protein. Conformational dependence on environment of an intrinsically unstructured protein. FEBS Journal (2006), 273:601-614

2004

  • Libich, David S; Robertson, Valerie J; Monette, Martine M; Harauz, George; Letter to the Editor: Backbone Resonance Assignments of the 18.5 kDa isoform of Murine Myelin Basic Protein (MBP), J. Biomol. NMR, 29, 545-546, (2004)