Y. Pankratova, M.J. McKay, C. Ma, H. Tan, J. Wang, and M. Hong, “Structure and Dynamics of the Proton-Selective Histidine and the Gating Tryptophan in an Inward Rectifying Hybrid Influenza B and A Virus M2 Proton Channel”, Phys. Chem. Chem. Phys.submitted (2024).


P. Duan, N. El Mammeri and M. Hong,  “Milligram-Scale Assembly and NMR Fingerprint of Tau Fibrils Adopting the Alzheimer’s Disease Fold”, J. Biol. Chem. 107326 (2024).


D. Tryfona, Y. Pankratova, P. Duan, M. Hong, and P. Dupree, “Altering the substitution and cross-linking of glucuronoarabinoxylans affects cell wall architecture in Brachypodium distachyon“, New Phytologist, 2024.


P. Duan and M. Hong, “Selective Detection of Intermediate-Amplitude Motion by Solid-State NMR“, J. Phys. Chem., 128, 2293−2303 (2024).


I. Sucec, Y. Pankratova, and M. Hong, “Transmembrane Conformation of the Envelope Protein of an Alpha Human Coronavirus, NL63“, Protein Science, 33, e4923 (2024).


N. El Mammeri$, A.J. Dregni$, P. Duan and M. Hong, “Structures of AT8 and PHF1 Phospho-Mimetic Tau: Insights into the Posttranslational Modification Code of Tau Aggregation“, Proc. Natl. Acad. Sci. U.S.A, 121,  e2316175121 (2024).




Duan, A.J. Dregni, N. El Mammeri and M. Hong, “Structure of the Non-Helical Filament of the Alzheimer’s Disease Tau Core “, Proc. Natl. Acad. Sci. U.S.A. 120, e2310067120 (2023).


J. Medeiros-Silva, A. J. Dregni, N. H. Somberg, and M. Hong, “Atomic Structure of the Open SARS-CoV-2 E Viroporin“, Sci. Advances, 9, eadi9007 (2023).


N. H. Somberg, J. Medeiros-Silva, H. Jo, J. Wang, W. F. DeGrado, and M. Hong, “Hexamethylene Amiloride Binds the SARS-CoV-2 Envelope Protein at the Protein-Lipid Interface “, Protein Science, e4755 (2023).


I. Sučec, N. El Mammeri, A.J. Dregni, and M. Hong, “Rapid Determination of the Topology of Oligomeric α‑Helical Membrane Proteins by Water- and Lipid-Edited Methyl NMR“, J. Phys. Chem. B, 127, 7518-7530 (2023).



N. El Mammeri, P. Duan, A.J. Dregni, and M. Hong, “Amyloid Fibril Structures of Tau: Conformational Plasticity of the Second Microtubule-Binding Repeat“, Sci. Adv., 9, eadh4731 (2023)


N. El Mammeri, O. Gampp, P. Duan and M. Hong, “Membrane-Induced Tau Amyloid Fibrils“, Commun. Biol. 6, 467 (2023).


A. A. Shcherbakov, M. Brousseau, K. A. Henzler-Wildman, and M. Hong, “Microsecond Motion of the Bacterial Transporter EmrE in Lipid Bilayers“, J. Am. Chem. Soc. 145, 10104-10115 (2023).


T. Kratochvil, L.C. Watkins, M. Mravic, N.H. Somberg, J.L. Thomaston, J. M. Nicoludis, Lijun Liu, M. Hong, G. A. Voth, W.F. DeGrado, “Transient Water Wires Mediate Selective Proton Transport in Designed Channel Proteins“. Nature Chem. 15, 1012-1021 (2023).


A. J. Dregni, M.J. McKay, W. Surya, M. Queralt-Martin, J. Medeiros-Silva, H. K. Wang, V. Aguilella, J. Torres, M. Hong*, The Cytoplasmic Domain of the SARS-CoV-2 Envelope Protein Assembles into a b-Sheet Bundle in Lipid Bilayers, J. Mol. Biol. 435, 167966 (2023).



S. Kim, M. Lee, M. Hong, and N. Holten-Andersen, “Quantitative Correlation between Bound Water and Mechanical Stress-relaxation in Dehydrated Metal-Coordinate Polymer Networks“, Chem. Materials, 34, 10329-10337 (2022).


N.H. Somberg, W. W. Wu, J. Medeiros-Silva, H. Jo, W. F. DeGrado, and M. Hong “The SARS-CoV-2 Envelope Protein Forms Pentamers in Lipid Bilayers“, Biochemistry, 61, 2280-2294 (2022).


N. El-Mammeri, A.J. Dregni, P. Duan, H. K. Wang, and M. Hong, “Microtubule-binding core of the tau protein“, Sci. Adv. 8, eabo4459 (2022)


A. J. Dregni$, P. Duan$, H. Xu, L. Changolkar, N. El Mammeri, V.M.-Y. Lee, and M. Hong, “Fluent Molecular Mixing of Tau Isoforms in Alzheimer’s Disease Neurofibrillary Tangles“, Nat. Commun. 13, 2967 (2022).


J. Medeiros-Silva, N. Somberg, H. K. Wang, M.J. McKay, V.S. Mandala, A.J. Dregni, and M. Hong, “pH- and Calcium-Dependent Aromatic Network in the SARS-CoV-2 Envelope Protein“, J. Am. Chem. Soc., 144, 6839-6850 (2022).


M. Sutherland, N. Tran, and M. Hong, “Clustering of the Influenza M2 Protein in Lipid Bilayers Investigated by 19F Solid-State NMR”, Biochim. Biophys. Acta, 1864, 183909 (2022).


H.S. Temple, P. Phyo, W. Yang, A. Echevarria-Poza, J. Lyczakowski, I. Yakunin, R. Dupree, A. Orellana, M. Hong and P. Dupree, “Discovery of putative Golgi S-Adenosyl methionine transporters reveals the importance of plant cell wall polysaccharide methylation”, Nat. Plants, 8, 656 (2022).


A.A. Shcherbakov, P.J. Spreacker, A.J. Dregni, K.A. Henzler-Wildman and M. Hong, “High-pH structure of EmrE reveals the mechanism of proton-coupled transport”, Nat. Commun., 13, 991 (2022).


P. Duan, K. J. Chen, G. Wijegunawardena, A.J. Dregni, H.K. Wang, H. Wu, and M. Hong, Binding Sites of a Positron Emission Tomography Imaging Agent in Alzheimer’s b-Amyloid Fibrils Studied Using 19F Solid-State NMR, J. Am. Chem. Soc. 144, 1416-1430 (2022).


A.A. Shcherbakov$, J. Medeiros-Silva$, N. Tran, M.D. Gelenter, and M. Hong, “From Angstroms to Nanometers: Measuring Interatomic Distances in Solid-State NMR”, Chemical Reviews, 122, 9848-9879 (2022).



N. Tran, Y. Oh, M. Sutherland, Q. Cui, and M. Hong, “Cholesterol-mediated clustering of the HIV fusion Protein gp41 in lipid bilayers”, J. Mol. Biol., 434 (2), 167345 (2021).


M.D. Gelenter, K.J. Chen and M. Hong, “Off-Resonance 13C-2H REDOR NMR for Site-Resolved Studies of Molecular Motion”, J. Biomol. NMR, 75, 335-345 (2021).


M. Sutherland, B. Kwon, and M. Hong, “Interactions of HIV gp41’s membrane-proximal external region and transmembrane domain with lipid membranes from 31P NMR”, Biochim. Biophys. Acta, 1863, 183723 (2021).


M.D. Gelenter, A.J. Dregni, P. Duan and M. Hong, “Structurally based design of glucagon mutants that inhibit fibril formation”, Biochemistry, 60, 2033-2043 (2021).


P. Duan, S.J. Kaser, J. J. Lyczakowski, P. Phyo, T. Tryfona, P. Dupree, and M. Hong “Developmental-Stage Dependent Xylan Structure and Dynamics in Brachypodium Cell Walls”, ACS Omega, 6, 15460-15471 (2021).


N.H. Somberg, M.D. Gelenter and M. Hong, “Comparative Analysis of 13C Chemical Shifts of b-sheet Amyloid Proteins and Membrane Proteins”, J. Biomol. NMR, 75, 151-166 (2021).


A.J. Dregni, H. K. Wang, H. Wu, P. Duan, W.F. DeGrado and M. Hong, “Inclusion of the C-Terminal Domain in the Tau Amyloid Fibril Core Revealed by Solid-State NMR Spectroscopy”, J. Am. Chem. Soc., 143, 7839-7851 (2021).


M.R. Elkins, A. Bandara, G.A. Pantelopulous, J. E. Straub, and M. Hong, Direct Observation of Cholesterol Dimers and Tetramers in Lipid BilayersJ. Phys. Chem. B., 125 (7), 1825-1837 (2021).


B. Reif, S. E. Ashbrook, L. Emsley, and M. Hong, “Solid-State NMR Spectroscopy”, Nature Reviews Methods Primers, 1, 2 (2021).


A.A. Shcherbakov, G. S. Hisao, V.S. Mandala, N. E. Thomas, M. Soltani, E. A. Salter, J. H. Davis Jr., K. Henzler-Wildman and M. Hong, “Drug-Binding Structure and Drug Dynamics of the Bacterial Transporter EmrE in Lipid Bilayers”, Nat. Comm., 12, 172 (2021).



V.S. Mandala, D. Loh, S.M. Shepard, M.B. Geeson, I.V. Sergeyev, D.G. Nocera, C. C. Cummins, and M. Hong, “Bacterial phosphate granules contain cyclic polyphosphates: Evidence from 31P solid-state NMR”, J. Am. Chem. Soc. 142, 18407-18421 (2020)



A.J. Dregni$, P. Duan$, and M. Hong, “Hydration and Dynamics of Full-Length Tau Amyloid Fibrils Investigated by Solid-State NMR”, Biochemistry, 59, 2237-2248 (2020).


M.D. Gelenter, A.J. Dregni, and M. Hong, “Pulsed Third-Spin-Assisted Recoupling NMR for Obtaining Long-Range 13C-13C and 15N-13C Distance Restraints”, J. Phys. Chem., 124, 7138-7151 (2020).


A.A. Shcherbakov, M. Roos, B. Kwon, and M. Hong, “Two-dimensional 19F-13C correlation NMR for 19F resonance assignment of fluorinated proteins”, J. Biomol. NMR, 74, 193-204 (2020).


V.S. Mandala, A.R. Loftis, A.A. Shcherbakov, B.L. Pentelute,  and M. Hong, “Atomic structures of closed and open influenza B M2 proton channel reveal the conduction mechanism”, Nat. Struct. Mol. Biol., 27 (2), 160-167 (2020).

Featured in MIT News: Chemists unveil the structure of an influenza B protein: Findings could help researchers design drugs to treat influenza B infections.



M. Lee$, C. A. Morgan$, and M. Hong, “Fully hydrophobic HIV gp41 adopts a hemifusion-like conformation in phospholipid bilayers ”, J. Biol. Chem., 294, 14732-14744 (2019).


M.D. Gelenter, K.J. Smith$, S.Y. Liao$, V.S. Mandala, A.J. Dregni, M.S. Lamm, Y. Tian, W. Xu, D.J. Pochan, T.J. Tucker, Y. Su, and M. Hong, “The peptide hormone glucagon forms amyloid fibrils with two coexisting β-strand conformations”, Nat. Struct. Mol. Biol., 26, 592-598 (2019).

Featured in MIT News: Chemists discover structure of glucagon fibrils: Study may be a step toward shelf-stable versions of the hormone, which is used to control diabetes.


B. Kwon$, M. Roos$, V.S. Mandala, A.A. Shcherbakov, and M. Hong, “Elucidating Relayed Proton Transfer Through a His-Trp-His Triad of a Transmembrane Proton Channel by Solid-State NMR”, J. Mol. Biol., 431, 2554-2566 (2019).


A.A. Shcherbakov, V.S. Mandala and M. Hong, “High-Sensitivity Detection of Nanometer 1H-19F Distances for Protein Structure Determination by 1H-Detected Fast MAS NMR”, J. Phys Chem. B, 123, 4387-4391 (2019).


M.R. Elkins and M. Hong, “Elucidating Ligand-Bound Structures of Membrane Proteins Using Solid-State NMR Spectroscopy”, Curr. Opin. Struct. Biol., 57, 103-109 (2019).


V.S. Mandala, S.Y. Liao, M.D. Gelenter and M. Hong, “Backbone Conformation of the Influenza Virus B M2 Protein in Lipid Bilayers from Solid-State NMR”, Sci. Rep., 9, 3725 (2019).


V.S. Mandala and M. Hong, “High-sensitivity protein solid-state NMR spectroscopy”, Curr. Opin. Struc. Biol., 58, 183-190 (2019).



M.R. Elkins, I.V. Sergeyev, and M. Hong, “Determining Cholesterol Binding to Membrane Proteins by Cholesterol 13C Labeling in Yeast and Dynamic Nuclear Polarization NMR”, J. Am. Chem. Soc., 140, 15437-15449 (2018).


M.K. Roos$, V.S. Mandala$, and M. Hong, “Determination of Long-Range Distances by Fast Magic-Angle-Spinning Radiofrequency-Driven 19F-19F Dipolar Recoupling NMR”, J. Phys. Chem. B, 122 (40), 9302-9313 (2018). ($ indicates equal contribution)


B. Kwon$, M. Lee$, A.J. Waring, and M. Hong, “Oligomeric Structure and Three-Dimensional Fold of the HIV gp41 MPER and Transmembrane Domain in Phospholipid Bilayers”, J. Am. Chem. Soc., 140 (26), 8246-8259 (2018).


M. Roos, T. Wang, A. A. Shcherbakov, M. Hong. “Fast Magic-Angle-Spinning 19F Spin Exchange NMR for Determining Nanometer 19F-19F Distances in Proteins and Pharmaceutical Compounds“, J. Phys. Chem. B 122 (11), 2900-2911 (2018). doi: 10.1021/acs.jpcb.8b00310.


P. Phyo, T. Wang, H. O’Neil, and M. Hong, “Direct Determination of Hydroxymethyl Conformations of Plant Cell Wall Cellulose Using 1H Polarization Transfer Solid-State NMR”, Biomacromolecules, 19 (5), 1485-1497 (2018). doi: 10.1021/acs.biomac.8b00039


V. S. Mandala, J. K. Williams, and M. Hong, “Structure and Dynamics of Membrane Proteins from Solid-State NMR”, Annu. Rev. Biophys. 47, 201-222 (2018).


S. Y. Liao, M. W. Lee, and M. Hong, “Interplay Between Membrane Curvature and Protein Conformational Equilibrium Investigated by Solid-State NMR”, J. Struct. Biol. Epub ahead of print (2018). doi: 10.1016/j.jsb.2018.02.007.


V. S. Mandala, M. D. Gelenter, M. Hong, “Transport-Relevant Protein Conformational Dynamics and Water Dynamics on Multiple Time Scales in an Archetypal Proton Channel: Insights from Solid-State NMR”, J. Am. Chem. Soc.  140, 1514-1524 (2018).  doi: 10.1021/jacs.7b12464.


H. Yang, T. Wang, D. Oehme, L. Petridis, M. Hong and J. D. Kubicki, “Structural factors affecting 13C NMR chemical shifts of cellulose – A computational study”, Cellulose, 25, 23-36 (2018).



P. Phyo, T. Wang, S. Kiemle, Hugh O’Neill, Sai V. Pingali, M. Hong, and D.J. Cosgrove, “Gradients in wall mechanics and polysaccharides along growing Arabidopsis inflorescence stems”, Plant Physiology , 175, 1593-1607 (2017).


M.R. Elkins, J. K. Williams, M. D. Gelenter, P. Dai, B.S. Kwon, I.V. Sergeyev, B.L. Pentelute, and M. Hong, “Cholesterol Binding Site of the Influenza M2 Protein in Lipid Bilayers from Solid-State NMR”, Proc. Natl. Acad. Sci. USA 114 (49), 12946-12951 (2017).

Featured in The Boston GlobeMIT researchers gain new insight on how flu spreads from cell to cell in the body

Featured in MIT News: Cholesterol helps flu virus escape through host cell’s membrane: Study could shed light on how many other proteins bind with membrane cholesterol.


J. K. Williams, A. A. Shcherbakov, J. Wang, M. Hong, “Protonation Equilibria and Pore-opening Structure of the Dual-histidine Influenza B Virus M2 Transmembrane Proton Channel from Solid-state NMR“, J. Biol. Chem. 292 (43), 17876-17884 (2017).


P. Phyo, T. Wang, C. Xiao, C. Anderson, and M. Hong, “Effects of pectin mutations on the structure of plant primary cell walls: insights from solid-state NMR”, Biomacromolecules 18, 2937-2950 (2017).


P. Dai, J. K. Williams, C. Zhang, M. Welborn, J. J. Shepherd, T. Zhu, T. Van Voorhis, M. Hong, B. L. Pentelute, “A Structural and Mechanistic Study of π-Clamp-Mediated Cysteine Perfluoroarylation“, Sci. Rep. 7, 7954 (2017).


M. D. Gelenter, T. Wang, S. Liao, H. O’Neill, M. Hong, “2H-13C Correlation Solid-State NMR for Investigating Dynamics and Water Accessibilities of Proteins and Carbohydrates“, J. Biomol. NMR. 68 (4), 257-270  (2017).


T. Wang and M. Hong, “Structure and Dynamics of Polysaccharides in Plant Cell Walls From Solid-State NMR”, Chapter 13, NMR in Glycoscience and Glycotechnology Royal Society of Chemistry (2017).


V. S. Mandala, S. Liao, B. Kwon and M. Hong, “Structural Basis of Inward Rectification in the Influenza M2 Proton Channel from Solid-State NMR”,  J. Mol. Biol. 429, 2192-2210 (2017).


M. Lee, T. Wang, O. V. Makhlynets, Y. Wu, N. Polizzi, H. Wu, J. Stöhr, I. V. Korendovych, W. F. DeGrado, and M. Hong, “Zinc-Binding Structure of a Catalytic Amyloid from Solid-State NMR Spectroscopy”, Proc. Natl. Acad. Sci. USA. 114 (24), 6191-6196 (2017).

Featured in MIT News: Chemists reveal amyloid structure: Discovery of how amyloids bind metal ions sheds light on protein function.


T. Wang, H. Jo, W.F. DeGrado, M. Hong, “Water Distribution, Dynamics and Interactions with Alzheimer’s Beta-Amyloid Fibrils Investigated by Solid-State NMR“, J. Am. Chem. Soc. 139 (17), 6242-6252 (2017).


D. Chen, M.D. Gelenter, M. Hong, R.E. Cohen, G.H. McKinley, “Icephobic Surfaces Induced by Interfacial Non-frozen Water“, ACS Appl. Mater. Interfaces 9 (4), 4202-4214 (2017).



R. Liang, J.M. Swanson, J.J. Madsen, M. Hong, W.F DeGrado and G.A. Voth, “Acid Activation Mechanism of the Influenza A M2 Proton Channel“, Proc. Natl. Acad. Sci. USA. 113, E6955-E6964 (2016).


T. Wang, Y. Chen, A. Tabuchi, D.J. Cosgrove and M. Hong, “The Target of Beta-Expansion EXPB1 in Maize Cell Walls from Binding and Solid-State NMR Studies”, Plant Physiol. 172, 2107-2119 (2016).


T. Wang, P. Phyo, M. Hong, “Multidimensional Solid-State NMR Spectroscopy of Plant Cell Walls“, Solid State Nucl. Magn. Reson. 78, 56-63 (2016).


M.R. Elkins, T. Wang, M. Nick, H. Jo, T. Lemmin, S. Prusiner, W.F. DeGrado, J. Stohr, M. Hong, “Structural Polymorphism of Alzheimer’s Beta-Amyloid Fibrils as Controlled by an E22 Switch: A Solid-State NMR Study“, J. Am. Chem. Soc. 138, 9840-9852 (2016).


J.K. Williams, D. Tietze, M. Lee, J. Wang, M. Hong, “Solid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton Channel“, J. Am. Chem. Soc. 138, 8143-8155 (2016).


S. Liao, M. Lee, T. Wang. I.V. Sergeyev and M. Hong, “Efficient DNP NMR of Membrane Proteins: Sample Preparation Protocols, Sensitivity, and Radical Location“, J. Biomol. NMR 64, 223-237 (2016).



J.K. Williams, K. Schmidt-Rohr and M. Hong, “Aromatic Spectral Editing Techniques for Magic-Angle-Spinning Solid-State NMR Spectroscopy of Uniformly 13C-Labeled Proteins“, Solid State Nucl. Magn. Reson. 72, 118-126 (2015).


H. Yao, M.W. Lee, A.J. Waring, G.C.L. Wong, and M. Hong, “A Viral Fusion Protein Transmembrane Domain Adopts β-Strand Structure to Facilitate Membrane Topological Changes for Virus-Cell Fusion“, Proc. Natl. Acad. Sci. USA, 112, 10926-10931 (2015).


T. Wang, Y.B. Park, D.J. Cosgrove, and M. Hong, “Cellulose-Pectin Spatial Contacts are Inherent to Never-Dried Arabidopsis thaliana Primary Cell Walls: Evidence from Solid-State NMR”, Plant Physiol. 168, 871-884 (2015).


B.S. Kwon, D. Tietze, P.B. White, S. Liao and M. Hong, “Chemical Ligation of the Influenza M2 Protein for Solid-State NMR Characterization of the Cytoplasmic Domain”, Protein Sci24, 1087-1099 (2015).


Y. Yang, H. Yao and M. Hong, Distinguishing Bicontinuous Lipid Cubic Phases from Isotropic Membrane Morphologies Using 31P Solid-State NMR Spectroscopy“, J. Phys. Chem. B 119, 4993-5001 (2015).


T. Wang, J.K. Williams, K. Schmidt-Rohr and M. Hong, Relaxation-Compensated Difference Spin Diffusion NMR for Detecting 13C-13C Long-Range Correlations in Proteins and Polysaccharides“, J. Biomol. NMR 61, 97-107 (2015).



145. N. Joh, T. Wang, M. Bhate, R. Acharya, Y. Wu, M. Grabe*, M. Hong*, G. Grigoryan* and W.F. DeGrado*, “De Novo Design of a Transmembrane Zn(II) Transporting Four-Helix Bundle”Science 346, 1520-1524 (2014). News and Events, Chemistry Department C&EN Science and Technology News, Dec 22, 2014.


J.K. Williams and M. Hong, “Probing Membrane Protein Structure Using Water Polarization Transfer Solid-State NMR”, J. Magn. Reson. 247, 118-127 (2014).


P.B. White, T. Wang, Y.B. Park, D.C. Cosgrove and M. Hong, “Hydration of Cellulose and Matrix Polysaccharides in the Primary Cell Wall of Arabidopsis Thaliana from Spin Diffusion NMR”, J. Am. Chem. Soc.136, 10399-409 (2014).


T. Wang, O. Zabotina, and M. Hong, “Structure and Dynamics of Brachypodium Primary Cell Wall Polysaccharides from Solid-State NMR Spectroscopy”, Biochemistry 53, 2840-2854 (2014).



Y. Yang, K.J. Fritzsching, and M. Hong, “Resonance Assignment of Disordered Proteins Using a Multi-Objective Non-Dominated Sorting Genetic Algorithm”, J. Biomol. NMR 57, 281-96 (2013).


S. Liao, K.J. Fritzsching, and M. Hong, “Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR”, Protein Sci. 22, 1623-38 (2013).


T. Wang, Y.B. Park, M.A. Caporini, M. Rosay, D.J. Cosgrove and M. Hong, “Sensitivity-Enhanced Solid-State NMR Detection of Expansin’s target in Plant Cell Walls”, Proc. Natl. Acad. Sci. U.S.A. 110, 16444-9 (2013).


R.L. Johnson, J.M. Anderson, B.H. Shanks, X. Fang, M. Hong, K. Schmidt-Rohr, “Spectrally edited 2D 13C-13C NMR spectra without diagonal ridge for characterizing 13C-enriched low-temperature carbon materials”, J. Magn. Reson. 234C, 112-124 (2013).


J.K. Williams, D. Tietze, J. Wang, Y. Wu, W.F. DeGrado and M. Hong, “Drug-Induced Conformational and Dynamical Changes of the S31N Mutant of the Influenza M2 Proton Channel Investigated by Solid-State NMR”, J. Am. Chem. Soc. 135, 9885-9897 (2013).



J. Williams, Y. Zhang, K. Schmidt-Rohr, and M. Hong, “Solid-state NMR investigation of the pH-dependent structure and dynamics of the gating residue of the influenza M2 proton channel”, Biophys. J. 104, 1698-1708 (2013). New and Notable commentary on 1639-1640.


M. Hong and K. Schmidt-Rohr, “Magic-Angle-Spinning NMR Techniques for Measuring Long-Range Distances in Biological Macromolecules”, Acct. Chem. Res. 46, 2154-63 (2013).




T. Wang, O. Zabotina, and M. Hong, “Pectin-cellulose and protein-polysaccharide  interactions in Arabidopsisprimary cell walls by 2D 13C Correlation NMR”, Biochemistry 51, 9846-9856 (2012).


T. Wang, L. Widanapathirana, Y. Zhao and M. Hong, “Aggregation and Dynamics of Oligocholate Transporters in Phospholipid Bilayers Revealed by Solid-State NMR Spectroscopy”, Langmuir 28, 17071-17078 (2012).


K. Schmidt-Rohr, K. J. Fritzsching, S. Liao, M. Hong, “Spectral Editing of Two-Dimensional Magic-Angle-Spinning Solid-State NMR Spectra for Protein Resonance Assignment and Structure Determination”, J. Biomol. NMR 54, 343-353 (2012).


M. Hong and W.F. DeGrado, “Structural Basis For Proton Conduction and Inhibition by the Influenza M2 Protein”, Invited review, Protein Sci. 21, 1620-1633 (2012).


S. Li, Y. Su, and M. Hong, “Intramolecular 1H-13C distance measurement in uniformly 13C, 15N labeled peptides by solid-state NMR”, Solid State Nucl. Magn. Reson. 45-46, 51-58 (2012).


M. Hong, K.J. Fritzsching, and J. K. Williams, “Hydrogen-Bonding Partner of the Proton-Conducting Histidine in the Influenza M2 Proton Channel Revealed From 1H Chemical Shifts”, J. Am. Chem. Soc. 134, 14753-5 (2012).


M. Dick-Perez, T. Wang, A. Salazar, O. Zabotina, and M. Hong, “Multidimensional Solid-State NMR Studies of the Structure and Dynamics of Pectic Polysaccharides in Uniformly 13C-Labeled Arabidopsis Primary Cell Walls”,Magn. Reson. Chem. 50, 539-550 (2012).


D.M. Harris, K. Corbin, T. Wang, R. Gutierrez,  A.L. Bertolo, C. Petti, D.M. Smilgies, J. M. Estevez, D. Bonetta, B. Urbanowicz, D. Ehrhardt, C.R. Somerville, J. K.C. Rose, M. Hong, S. DeBolt, “Cellulose microfibril crystallinity is reduced by mutating C-terminal transmembrane region residues CESA1A903V and CESA3T942I of cellulose synthase”, Proc. Natl. Acad. Sci. U.S.A. 109, 4098-4103 (2012).


F. Hu, K. Schmidt-Rohr and M. Hong, “NMR Detection of pH-Dependent Histidine-Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel”, J. Am. Chem. Soc. 134, 3703-3713 (2012). Cover of JACS volume 134, issue 8.


M. Hong, Y. Zhang and F. Hu, “Membrane protein structure and dynamics from NMR spectroscopy”, Review,Annu. Rev. Phys. Chem. 63, 1-24. (2012).




J. Wang, C. Ma, G. Fiorin, V. Carnevale, T. Wang, F. Hu, R.A. Lamb, M.L. Klein, L.H. Pinto, M. Hong, and W.F. DeGrado, “Molecular Dynamics Simulation Directed Rational Design of Inhibitors Targeting Drug-Resistant Mutants of Influenza A Virus M2”, J. Am. Chem. Soc. 133, 12834-12841 (2011).


S.D. Cady, T. Wang, and M. Hong, “Membrane-Dependent Effects of a Cytoplasmic Helix on the Structure and Drug Binding of the Influenza M2 Protein”, J. Am. Chem. Soc. 133, 11572-11579 (2011).


M. Hong and Y. Su, “Structure and Dynamics of Cationic Membrane Peptides and Proteins: Insights from Solid-State NMR”, Protein Sci. review, 20, 641-655 (2011).


M. Dick-Perez, Y. Zhang, J. Hayes, A. Salazar, O.A. Zabotina and M. Hong, “Structure and Interactions of Plant Cell-Wall Polysaccharides by 2D and 3D Magic-Angle-Spinning Solid-State NMR”, Biochemistry 50, 989-1000 (2011).




F. Hu, W. Luo, and M. Hong, “Mechanisms of proton conduction and gating by influenza M2 proton channels from solid-state NMR”, Science 330, 505-508 (2010).


T. Doherty*, Y. Su* and M. Hong, “High-Resolution Orientation and Depth of Insertion of the Voltage-Sensing S4 Helix of a Potassium Channel in Lipid Bilayers”, J. Mol. Biol. 401, 642-652 (2010). (* indicates equal contribution)


W. Luo and M. Hong, “Conformational Changes of an Ion Channel Detected Through Water-Protein Interactions Using Solid-State NMR”, J. Am. Chem. Soc. 132, 2378-2384 (2010).


S.D. Cady, K. Schmidt-Rohr, J. Wang, C.S. Soto, W.F. DeGrado, and M. Hong, “Structure of the amantadine binding site of influenza M2 proton channels In lipid bilayers”, Nature 463, 689-692 (2010).


Y. Zhang, T. Doherty, J. Li, W. Lu, C. Barinka, J. Lubkowski and M. Hong, “Resonance Assignment and Three-Dimensional Structure Determination of a Human Alpha-Defensin, HNP-1, by Solid-State NMR”, J. Mol. Biol. 397, 408-422 (2010).



S.D. Cady, W. Luo, F. Hu, and M. Hong, “Structure and function of the influenza M2 proton channel”, Current TopicBiochemistry 48, 7356-7364 (2009).


J. Wang, S.D. Cady, V. Balannik, L.H. Pinto, W.F. DeGrado, and M. Hong, “Discovery of Spiro-piperidine inhibitors and their modulation of the dynamics of the M2 proton channel from influenza A Virus”, J. Am. Chem. Soc. 131, 8066-8076 (2009).


M. Tang. and M. Hong. “Structure and Mechanism of β-Hairpin Antimicrobial Peptides in Lipid Bilayers from Solid-State NMR Spectroscopy”, Mol. Biosys. 5, 317-322 (2009).


M. Tang, A.J. Waring and M. Hong, “Effects of Arginine Density on the Membrane-Bound Structure of a Cationic Antimicrobial Peptide from Solid-State NMR”, Biochim. Biophys. Acta 1788, 514-521 (2009).



Y. Su, R. Mani, T. Doherty, A.J. Waring and M. Hong, “Reversible Sheet – Turn Conformational Change of a Cell-Penetrating Peptide in Lipid Bilayers Studied by Solid-State NMR“, J. Mol. Biol. 381,1133 -1144 (2008).


M. Tang, A.J. Waring, and M. Hong, “Arginine Dynamics in a Membrane-Bound Cationic Beta-Hairpin Peptide from Solid-State NMR“, ChemBioChem 9, 1487-1492 (2008).


M. Tang, A.J. Waring, R.I. Lehrer and M. Hong, “Effects of Guanidinium-Phosphate Hydrogen Bonding on the Membrane-Bound Structure and Activity of an Arginine-Rich Membrane Peptide from Solid State NMR“, Angew. Chem. Int. Ed. Engl. 47, 3202-3205 (2008).


S.D. Cady and M. Hong, “Amantadine-Induced Conformational and Dynamical Changes of the Influenza M2 Transmembrane Proton Channel“, Proc. Natl. Acad. Sci. U.S.A. 105, 1483-1488 (2008).


T. Doherty, A.J. Waring and M. Hong, “Dynamic Structure of Disulfide-Removed Linear Analogs of Tachyplesin-I in the Lipid Bilayer from Solid-State NMR“, Biochemistry 47, 1105-1116 (2008).



M. Hong, “Structure, Topology, and Dynamics of Membrane Peptides and Proteins from Solid-State NMR Spectroscopy“, J. Phys. Chem. B feature article, 111, 10340-10351 (2007).


W. Luo, R. Mani and M. Hong, “Sidechain Conformation and Gating of the M2 Transmembrane Peptide Proton Channel of Influenza A Virus from Solid-State NMR“, J. Phys. Chem. B 111, 10825-10832 (2007).


M. Tang, A.J. Waring and M. Hong, “Trehalose-Protected Lipid Bilayers for Determining Membrane Protein Insertion and Topology“, J. Magn. Reson. 184, 222-227 (2007).


M. Tang, A.J. Waring and M. Hong, “Phosphate-Mediated Arginine Insertion Into Lipid Membranes and Pore Formation by a Cationic Membrane Peptide from Solid-State NMR“, J. Am. Chem. Soc. 129, 11438-11446 (2007).




T. Doherty, A.J. Waring and M. Hong, “Membrane-bound conformation and topology of Tachyplesin-1 by solid-state NMR spectroscopy“, Biochemistry, 45, 13323-13330 (2006).


R. Mani, S.D. Cady, M. Tang, A.J. Waring, R.I. Lehrer, and M. Hong, “Membrane-dependent oligomeric structure and pore formation of a β-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR“, Proc. Natl. Acad. Sci. U.S.A. 103, 16242-16247 (2006).


R. Mani, M. Tang, X. Wu, J.J. Buffy, A.J. Waring, M.A. Sherman, and M. Hong, “Membrane-Bound Dimer Structure of a β-Hairpin Antimicrobial Peptide from Rotational-Echo Double-Resonance Solid-State NMR“,Biochemistry 45, 8341-8349 (2006).


T. Doherty, A. Waring, and M. Hong, “Peptide-Lipid Interactions of the β-Hairpin Antimicrobial Peptide Tachyplesin and its Linear Derivatives from Solid-State NMR“, Biochim. Biophys. Acta 1758, 1285-1291 (2006).


W. Luo and M. Hong, “1D Sensitivity-Enhanced 1H Spin Diffusion Experiment for Determining Membrane Protein Topology“, Solid State Nuc. Magn. Reson. 29, 163-169 (2006).


M. Tang, A.J. Waring, R.I. Lehrer, and M. Hong, “Orientation of a β-hairpin Antimicrobial Peptide in Lipid Bilayers from 2D Dipolar Chemical-Shift Correlation NMR“, Biophys. J. 90, 3616-3624 (2006).



P.A.B. Marasinghe, J.J. Buffy, K. Schmidt-Rohr and M. Hong, “Membrane Curvature Change Induced by an Antimicrobial Peptide Detected by 31P Exchange NMR“, J. Phys. Chem. B 10922036-44 (2005).


M. Tang, A.J. Waring, and M. Hong, “Intermolecular Packing and Alignment of a β-Hairpin Peptide from 2D Solid-State NMR“,  J. Am. Chem. Soc. 127, 13919-13927 (2005).


R. Mani, A.J. Waring, R.I. Lehrer, and M. Hong, “Membrane-Disruptive Abilities of β-Hairpin Antimicrobial Peptides Correlate with Conformation and Activity: A 31P and 1H NMR Study“, Biochim. Biophys. Acta, 1716, 11-18 (2005).


J.J. Buffy, A.J. Waring, and M. Hong, “Determination of Peptide Oligomerization in Lipid Bilayers Using 19F Spin Diffusion NMR“, J. Am. Chem. Soc. 127, 4477-4483 (2005).


M. Hong and S. Wi, “Torsion Angle Determination in Biological Solids by Solid-State NMR”, chapter 4, NMR spectroscopy of Biological Solids, CRC Press, Boca Raton, 2005.



R. Mani, J.J. Buffy, A.J. Waring, R.I. Lehrer, and M. Hong, “Solid-State NMR Investigation of the Selective Disruption of Lipid Membranes by Protegrin-1“,  Biochemistry 43, 13839-48 (2004).


S. Wi, N. Sinha and M. Hong, “Long-range distances by heteronuclear detected 19F-1H rotational-echo double-resonance NMR“, J. Am. Chem. Soc. 126, 12754-5 (2004).


N. Sinha, K. Schmidt-Rohr and M. Hong, “Compensation for Pulse Imperfections in Rotational-Echo Double-Resonance NMR by Composite Pulses and EXORCYCLE“, J. Magn. Reson. 168, 358-65 (2004).


J.J. Buffy, M.J. McCormick, S. Wi, A. Waring, R.I. Lehrer, and M. Hong, “Selective Perturbation of Lipid Membranes by the Cyclic Antimicrobial Peptide RTD-1 Investigated by Solid-State NMR“, Biochemistry 43, 9800-9812 (2004).


A.T. Petkova, M. Baldus, M. Belenky, M. Hong, R.G. Griffin, J. Herzfeld, “Backbone and side chain assignment strategies for multiply labeled membrane peptides and proteins in the solid state“, J. Magn. Reson. 160: 1-12 (2003).


G.J. Gallagher, M. Hong, L.K. Thompson, “Solid-state NMR spin diffusion for measurement of membrane-bound peptide structure: gramicidin A“, Biochemistry 43, 7899-7906 (2004).


X.L. Yao and M. Hong, “Structural Distribution in an Elastin-Mimetic Peptide by Magic-Angle Spinning Solid-State NMR Spectroscopy“, J. Am. Chem. Soc. 126, 4199-4210 (2004).


X.L. Yao, R.A. McMillian, V.P. Conticello, and M. Hong, “Investigation of the Dynamics of an Elastin-Mimetic Polypeptide Using Solid-State NMR“, Magn. Reson. Chem. 42, 267-275 (2004).



N. Sinha and M. Hong, “X-1H Rotational-Echo Double-Resonance NMR For Torsion Angle Determination in Peptides”, Chem. Phys. Lett. 380, 742-748 (2003).


J. Buffy, A.J. Waring, R. I. Lehrer, and M. Hong, “Immobilization and Aggregation of Antimicrobial Peptide Protegrin in Lipid Bilayers by Solid-State NMR”, Biochemistry, 42, 13725-34 (2003).


K. Schmidt-Rohr and M. Hong, “Measurements of Carbon to Amide-Proton Distances by C-H Dipolar Recoupling with 15N NMR Detection”, J. Am. Chem. Soc. 125, 5648-5649 (2003).


J. Buffy, T. Hong, S. Yamaguchi, A. Waring, R.I. Lehrer, and M. Hong, “Solid-State NMR Investigation of the Depth of Insertion of PG-1 in DLPC Using Paramagnetic Mn2+”, Biophys. J. 85, 2363-2373 (2003).


M. Hong, D. Isailovic, R.A. McMillan, and V.P. Conticello, “Solid-state NMR chemical shift constraints for the structure of an elastin-mimetic protein”, Biopolymers, 70, 158-168, (2003).



X.L. Yao, S. Yamaguchi and M. Hong, “Ca Chemical Shift Tensors in Helical Peptides by Dipolar-Modulated Chemical Shift Recoupling NMR”, J. Biomol. NMR 24, 51-62 (2002).


S. Yamaguchi, A. Waring, T. Hong, R.I. Lehrer and M. Hong, “Solid-state NMR Investigations of Peptide-Lipid Interaction and Orientation of a β-sheet antimicrobial peptide, Protegrin”, Biochemistry 41, 9852-9862 (2002).


M. Hong, X.L. Yao, K. Jakes and D. Huster, “Investigation of Molecular Motions by Magic-Angle Cross-Polarization NMR Spectroscopy”, J. Phys. Chem. 106, 7355-7364 (2002).


D. Huster, X.L. Yao and M. Hong, “Membrane Protein Topology Probed by 1H Spin Diffusion from Lipids Using Solid-State NMR Spectroscopy”, J. Am. Chem. Soc. 124, 874-883 (2002).


M. Hong*, R.A. McMillan, and V.P. Conticello, “Measurement of Conformational Constraints in an Elastin-Mimetic Protein by Residue-Pair Selected Solid-State NMR”, J. Biomol. NMR 22, 175-179 (2002).


S. Yamaguchi and M. Hong, “Determination of Membrane Peptide Orientation by 1H-Detected 2H NMR”, J. Magn. Reson. 155, 244-250 (2002).


D. Huster, X.L. Yao, K. Jakes, and M. Hong, “Conformational changes of colicin Ia channel-forming domain upon membrane binding: a solid-state NMR study”, Biochim. Biophys. Acta 1561, 159-170 (2002).



S.B. Kennedy, E. de Azevedo, W.A. Petka, D.A. Tirrell, T.P. Russell, and M. Hong, “Dynamic Structure of a Protein Hydrogel: A Solid-State NMR Study”, Macromolecules 34, 8675-8685 (2001).


S. Yamaguchi, D. Huster, A. Waring, R.I. Lehrer, W. Kearney, B.F. Tack, and M. Hong, “Orientation and Dynamics of an Antimicrobial Peptide in the Lipid Bilayer by Solid-State NMR”, Biophys. J. 81, 2203-2214 (2001).


X.L. Yao and M. Hong, “Dipolar Filtered 1H-13C Heteronuclear Correlation Spectroscopy For Resonance Assignment of Proteins”, J. Biomol. NMR 20, 263-274 (2001).


X. L. Yao, K. Schmidt-Rohr, and M. Hong, “Medium- and Long-Distance 1H-13C Heteronuclear Correlation NMR in Solids”, J. Magn. Reson. 149, 139-143 (2001).


K. Schmidt-Rohr, K. Saalwächter, S. Liu, and M. Hong, “High-Sensitivity 2H-NMR in Solids by 1H Detection”, J. Am. Chem. Soc. 123, 7168-7169 (2001).


D. Huster, L.S. Xiao, and M. Hong, “Solid-State NMR Investigation of the Dynamics of Colicin Ia Channel-Forming Domain”, Biochemistry 40, 7662-7674 (2001).


M. Hong and S. Yamaguchi, “Sensitivity-Enhanced 15N Static NMR in Solids by 1H Indirect Detection”, J. Magn. Reson. 150, 43-48 (2001).

1999 – 2000


D. Huster, S. Yamaguchi, and M. Hong, “Efficient b-Sheet Identification in Proteins by Solid-State NMR spectroscopy”, J. Am. Chem. Soc. 122, 11320-11327 (2000).


C.M. Rienstra, M. Hohwy, M. Hong and R.G. Griffin, “2D and 3D 15N-13C-13C NMR chemical shift correlation spectroscopy of solids: assignment of MAS spectra of peptides”, J. Am. Chem. Soc. 122, 10979-10990 (2000).


D.J. Harris, T.J. Bonagamba, M. Hong and K. Schmidt-Rohr, “Conformation of Poly(ethylene oxide)-Hydroxybenzene Molecular Complexes Studied by Solid-state NMR”, Macromolecules 33, 3375-3381 (2000).


E.R. deAzevedo, S.B. Kennedy and M. Hong, “Determination of Slow Motions in Extensively Isotopically Labeled Proteins by Magic-Angle-Spinning 13C-Detected 15N Exchange NMR”, Chem. Phys. Lett. 321, 43-48 (2000).


M. Hong and K. Jakes, “Selective and Extensive 13C Labeling of a Membrane Protein for Solid-State NMR Investigation”, J. Biomol. NMR 14, 71-74 (1999).


D. Sandström, M. Hong and K. Schmidt-Rohr, “Identification and Mobility of Deuterated Sites in Peptides and Proteins by 2H-13C Correlation in Solid-State NMR”, Chem. Phys. Lett. 300, 213-220 (1999).

1997 – 1998


A.T. Petkova, M. Baldus, M. Belenky, M. Hong, R.G. Griffin, J. Herzfeld, “Backbone and side chain assignment strategies for multiply labeled membrane peptides and proteins in the solid state”, J Magn. Reson. 160, 1-12 (2003).


M. Hong, J.D. Gross, W. Hu and R.G. Griffin, “Determination of the Peptide Torsion Angle f by 15N Chemical Shift and 13Cα1Hα Dipolar Tensor Correlation in Solid-State MAS NMR“, J. Magn. Reson. 135, 169-177 (1998).


M. Hong and R.G. Griffin, “Resonance Assignments for Solid Peptides by Dipolar-Mediated 13C/15N Correlation Solid-State NMR”, J. Am. Chem. Soc. 120, 7113-7114 (1998).


P.R. Costa, J.D. Gross, M. Hong and R.G. Griffin, “A NCCN 2Q-HLF Experiment for Y Torsion Angle Measurements in Peptides”, Chem. Phys. Lett.  280, 95-103 (1997).


M. Hong, J.D. Gross, C.M. Rienstra, R.G. Griffin, K.K. Kumashiro and K. Schmidt-Rohr, “Coupling Amplification in 2D MAS NMR and its Application to Torsion Angle Determination in Peptides”, J. Magn. Reson. 129, 85-92 (1997).

1994 – 1996


S. Caldarelli, M. Hong, L. Emsley and A. Pines, “Measurement of Carbon-Proton Dipolar Coupling in Liquid Crystals by Local Dipolar Field NMR Spectroscopy”, J. Phys. Chem. 100, 18696-18701 (1996).


M. Hong, A. Pines and S. Caldarelli, “Measurement and Assignment of Long-Range C-H Dipolar Couplings in Liquid Crystals by Two-Dimensional NMR Spectroscopy”, J. Phys. Chem. 100, 14815-14822 (1996).


M. Hong, K. Schmidt-Rohr and Zimmerman H, “Conformational Constraints on the Headgroup and sn-2 Chain of Bilayer DMPC from NMR Dipolar Couplings”, Biochemistry 35, 8335-8341 (1996).


K. Schmidt-Rohr and M. Hong, “Information on Bond Orientation Distributions in Lipids and Liquid Crystals from Segmental Order Parameters”, J. Phys. Chem. 100, 3861-3866 (1996).


M. Hong, K. Schmidt-Rohr and D. Nanz, “Study of Phospholipid Structure by 1H, 13C, and 31P Dipolar Couplings from Two-Dimensional NMR”, Biophys. J. 69, 1939-1950 (1995).


M. Hong and K. Schmidt-Rohr, “DISTINCT NMR for Sign Determination of C-H Dipolar Couplings in Liquid-Crystalline Lipids”, J. Magn. Reson. B 109, 284-290 (1995).


M. Hong, K. Schmidt-Rohr and A. Pines, “NMR Measurement of Signs and Sizes of C-H Dipolar Couplings in Lecithin”, J. Am. Chem. Soc. 117, 3310-3311 (1995).


D. Nanz, M. Ernst, M. Hong, M.A. Ziegeweid, K. Schmidt-Rohr and A. Pines, “Low-Power Decoupling with Windowless Multiple-Pulse Sequences for High-Resolution Spectra of Orientationally Ordered Samples”, J. Magn. Reson. A 113,169-176 (1995).


Y.K. Lee, L. Emsley, R.G. Larsen, K. Schmidt-Rohr, M. Hong, L. Frydman, G.C. Chingas and A. Pines, “Three-Dimensional Variable-Angle Nuclear Magnetic Resonance Exchange Spectroscopy without Rotor Axis Hopping”, J. Chem. Phys. 101 (3), 1852-1864 (1994).

denotes equal contribution