Publications

For a complete list of Mei Hong's publications on Google Scholar, see here

2017

172. 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).
 
171. 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. Online First Article (2017).
                                        
170. 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). 
 
169. 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).
                                                  
 
168. 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”, PNAS, 114 (24), 6191-6196 (2017).
                                                                                        
167. 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).
                                                                 
 
166. 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).
                                                         

 

2016

165. 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).
                         
163. T. Wang, Y. Chen, A. Tabuchi, D.J. Cosgrove and M. Hong, "The Target of Beta-Expansin EXPB1 in Maize Cell Walls from Binding and Solid-State NMR Studies", Plant Physiol. 172, 2107-2119 (2016).
161.  T. Wang, P. Phyo, M. Hong, "Multidimensional Solid-State NMR Spectroscopy of Plant Cell Walls", Solid State Nucl. Magn. Reson. 78, 56-63 (2016).
159. M. 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).
158. 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).
157. 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).
 

2015

154. 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).
 
153. 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).
 
151. 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).
 
150. 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 Sci. 24, 1087-1099 (2015).
 
 
 
146. 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).
 
2014
 
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).
 
144. J.K. Williams and M. Hong, “Probing Membrane Protein Structure Using Water Polarization Transfer Solid-State NMR”, J. Magn. Reson. 247, 118-127 (2014).
 
 
142. 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).
 
141. 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).
 
 

2013

139. 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).
 
138. 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).
 
137. 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).
 
 
135. 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).
 
134. 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).
 
133. K.J. Fritzsching, Y. Yang, K. Schmidt-Rohr, and M. Hong, “Practical Use of Chemical Shift Databases for Protein Solid-State NMR: 2D Chemical Shift Maps and Amino-Acid Assignment with Secondary-Structure Information”, J. Biomol. NMR 56, 155-167 (2013).
 
 
131. 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.
 
130. 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).
 
 
 

2012

127. T. Wang, O. Zabotina, and M. Hong, “Pectin-cellulose and protein-polysaccharide  interactions in Arabidopsis primary cell walls by 2D 13C Correlation NMR”, Biochemistry 51, 9846-9856 (2012).
 
126. 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).
 
125. 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).
 
124. 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).
 
123. 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).
 
122. 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).
 
 
120. 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).
 
119. 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).
 
 
 
116. M. Hong, Y. Zhang and F. Hu, “Membrane protein structure and dynamics from NMR spectroscopy”, Review, Annu. Rev. Phys. Chem. 63, 1-24. (2012).
 

2011

115. Y. Su and M. Hong, “Conformational disorder of membrane peptides investigated from solid-state NMR line widths and line shapes”, J. Phys. Chem. 115, 10758-10767 (2011).
 
114. 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). 
 
113. 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).
 
112. 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).
 
 
 
109. 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).
 
 
107. F. Hu, W. Luo, S.D. Cady and M. Hong, “Conformational Plasticity of the Influenza A M2 Transmembrane Peptide in Lipid Bilayers Under Varying pH, Drug Binding and Membrane Thickness”, Biochim. Biophys. Acta 1808, 415-423 (2011).
 

2010

 
105. 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).
 
 
 
102. 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)
 
 
100.  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).
 
99. 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).
 
 
97. 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).
 

2009

96. S.D. Cady, W. Luo, F. Hu, and M. Hong, “Structure and function of the influenza M2 proton channel”, Current Topic, Biochemistry 48, 7356-7364 (2009).
 
 
 
 
 
91. 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).
 
 
89. 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). 
 
 
87. 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).
 
 

2008

85. 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).
 
 
83. 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).
 
82. 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).
 
 
80. 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).
 
79.  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).
 

 2007

 
77. 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).
 
 
 
74. 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).
 
 

 2006

 
 
70. 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).
 
69. 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).
 
68. 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).
 
 
66. 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).
 
 
 
63. 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).
 
62. 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).
 

2005

61. 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 109, 22036-44 (2005).
 
60. 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).
 
59. 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).
 
 
 
56. 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).
 
55. 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.
 

2004

54. 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).
 
53. 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).
 
52. 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).
 
51. 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).
 
50. 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).
 
49. 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).
 
 
47. 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).
 

2003

46. 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).
 
45. 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).
 
44. 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).
 
43. 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).
 
 
41. 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).
 

2002

40. 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).
 
39. 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).
 
38. 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).
 
 
36. 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).
 
35. 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).
 
34. S. Yamaguchi and M. Hong, “Determination of Membrane Peptide Orientation by 1H-Detected 2H NMR”, J. Magn. Reson. 155, 244-250 (2002).
 
33. 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).
 

2001

32. 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).
 
31. 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).
 
30. 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).
 
29. 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).
 
28. 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).
 
27. 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).
 
26. 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

25. 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).
 
24. M. Hong, “Solid-State NMR Determination of 13Cα Chemical Shift Anisotropy for the Identification of Protein Secondary Structure”, J. Am. Chem. Soc. 122, 3762-3770 (2000).
 
23. 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).
 
22. 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).
 
21. 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).
 
19. 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).
 
17. 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

15. 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).
 
14. M. Hong, J.D. Gross, W. Hu and R.G. Griffin, “Determination of the Peptide Torsion Angle f by 15N Chemical Shift and 13Cα-1Hα Dipolar Tensor Correlation in Solid-State MAS NMR", J. Magn. Reson. 135, 169-177 (1998).
 
13. 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).
 
12. 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).
 
11. 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

9. 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).
 
8. 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).
 
7. 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).
 
6. 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).
 
5. 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).
 
4. 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).
 
3. 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).
 
2. 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).
 
1. 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).