Protein NMR 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.