Group Picture (October 2019)
Robert Wolfe as a graduate research associate
Yijin Zhang as a graduate research associate
Md Rokonujjaman as a graduate research associate
Noel Chau as a graduate research associate
Ujjayini Ghosh as a postdoctoral research associate
Ahinsa Ranaweera (Ph. D. 2019, Senior Lecturer at Rajarata University of Sri Lanka)
Shuang Liang (Ph. D. 2017, Scientist at Alcon)
Lihui Jia (Ph. D. 2017, Scientist at Alcon)
Ujjayini Ghosh (Ph. D. 2016, Scientist at National Institutes of Health)
Punsisi Ratnayake (Ph. D. 2015) Scientist at Katahdin Analytical Services
Li Xie (Ph. D. 2014, Scientist at Michigan State University)
Koyeli Banerjee (Ph. D. 2014, Program Official at the National Institutes of Health)
Scott Schmick (Ph. D. 2013, Scientist at 3M)
Kelly Sackett (Scientist at Pfizer)
Erica Vogel (Ph. D. 2012) Owner of Be Like Missy boutique
Matthew Nethercott (Ph. D. 2012, Scientist at Kansas Analytical Services)
Yan Sun (Ph. D. 2009, Instructor at Binghamton University)
Wei Qiang (Ph. D. 2009, Professor at Binghamton University)
Jaime Curtis-Fisk (Ph. D. 2009, Scientist at Dow Chemical)
Matthew Gave (Ph. D. 2008, Scientist at Dow Chemical)
Zhaoxiong Zheng (Ph. D. 2007, Scientist at Shell Oil)
Michele Bodner (Ph. D. 2006, Scientist at Gilead)
Paul Parkanzky (Ph. D. 2006, Scientist at Amway)
Rong Yang (Ph. D. 2005, Scientist at National Institutes of Health)
Christian Canlas (Ph. D. 2004, Scientist at the King Abdullah University of Science & Technology)
Jun Yang (Ph. D. 2003, Scientist at Lerner Research Institute, Cleveland Clinic)
Bhagyashree Khunte (M. S. 2001, Scientist at Pfizer Corporation)
Dr. Weliky telephone: 517-353-1177
Graduate Student/Post-doc telephone: 517-353-1178
The Weliky group specializes in solid-state NMR spectroscopy with particular application to biological systems. Solid-state NMR is a powerful approach to structural and dynamical measurements on biological molecules and is particularly useful for studies in non-crystalline environments such as membranes and bacterial inclusion bodies. We spend about 80% of our effort on applications and 20% of our effort on new methods development. Our research includes physical, analytical, organic, and biological chemistries.
We are currently studying the structure of the membrane-associated HIV gp41 envelope protein. One project focuses on the fusion peptide region of gp41, which is required for viral/host cell membrane fusion. We are studying this peptide as well as the whole gp41 protein in the most biologically relevant membrane environment. Our goal is to better understand the structural basis of membrane fusion which should be useful for designing new AIDS therapeutics. We also have a related project on the influenza virus fusion protein.
A second area is the structure of recombinant proteins in bacterial inclusion bodies. Academic and pharmaceutical laboratories commonly produce large quantities of a protein by introducing the gene for this protein into E. coli bacteria and having the bacteria make the protein. A common problem is sequestration of the foreign protein in non-crystalline solids termed inclusion bodies. Better understanding of the protein structure in inclusion bodies should lead to better methods of obtaining useful protein from inclusion bodies.
We have two 400 MHz Varian Chemagnetics Infinity Plus spectrometers. In addition, we have a variety of magic angle spinning and static probes.
We have an incubator shaker, refrigerated centrifuges, preparative HPLC, FPLC, uv-vis spectrophotometer, and lyophilizer. We also have a nitrogen/vacuum line for organic derivatization of amino acids.
Publications (in pdf format)
1. U. Ghosh and D. P. Weliky, “2H Nuclear Magnetic Resonance Spectroscopy Supports Larger Amplitude Fast Motion and Interference with Lipid Chain Ordering for Membrane that Contains β Sheet Human Immunodeficiency Virus gp41 Fusion Peptide or Helical Hairpin Influenza Virus Hemagglutinin Fusion Peptide at Fusogenic pH”, Biochimica et Biophysica Acta- Biomembranes (2020) 1862, 183404.
A. Ranaweera, P. U. Ratnayake, E. A. P. Ekanayaka, R. Declercq, and D. P. Weliky, “Hydrogen−Deuterium Exchange Supports Independent Membrane-Interfacial Fusion Peptide and Transmembrane Domains in Subunit 2 of Influenza Virus Hemagglutinin Protein, a Structured and Aqueous-Protected Connection between the Fusion Peptide and Soluble Ectodomain, and the Importance of Membrane Apposition by the Trimer-of-Hairpins Structure”, Biochemistry (2019) 58, 2432-2466.
3. A. Ranaweera, P. U. Ratnayake, and D. P. Weliky, “The Stabilities of the Soluble Ectodomain and Fusion Peptide Hairpins of the Influenza Virus Hemagglutinin Subunit II Protein Are Positively Correlated with Membrane Fusion”, Biochemistry, 57, 5480-5493 (2018).
4. S. Liang, P. U. Ratnayake, C. Keinath, L. Jia, R. Wolfe, A. Ranaweera, and D. P. Weliky, “Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers Containing the Fusion Peptide and Transmembrane Domains”, Biochemistry, 57, 1219-1235 (2018).
P. N. Grenga, M. J. Nethercott, A. E. Mateo, M. Paternaude, T. Hoare, D. P. Weliky, and R. Priefer, “Thermal and Spectral Analysis of Novel Amide-Tethered Polymers from Poly(allylamine)”, Australian Journal of Chemistry, 69, 458-466 (2016).
6. P. U. Ratnayake, E. A. Prabodha Ekanayaka, S. S. Komanduru, and D. P. Weliky, “Full-Length Trimeric Influenza Virus Hemagglutinin II Membrane Fusion Protein and Shorter Constructs Lacking the Fusion Peptide or Transmembrane Domain: Hyperthermostability of the Full-Length Protein and the Soluble Ectodomain and Fusion Peptide Make Significant Contributions to Fusion of Membrane Vesicles”, Protein Expression and Purification, 117, 6-16 (2016).
U. Ghosh, L. Xie, L. Jia, S. Liang, and D. P. Weliky, “Closed and Semiclosed Interhelical Structures in Membrane vs Closed and Open Structures in Detergent for the Influenza Virus Hemagglutinin Fusion Peptide and Correlation of Hydrophobic Surface Area with Fusion Catalysis”, Journal of the American Chemical Society, 137, 7548-7551 (2015).
9. L. Jia, S. Liang, K. Sackett, L. Xie, U. Ghosh, and D. P. Weliky, “REDOR Solid-State NMR as a Probe of the Membrane Locations of Membrane-Associated Peptides and Proteins”, Journal of Magnetic Resonance, 253, 154-165 (2015).
10. L. Xie, L. Jia, S. Liang, and D. P. Weliky, “Multiple Locations of Peptides in the Hydrocarbon Core of Gel-Phase Membranes Revealed by Peptide 13C to Lipid 2H Rotational-Echo Double Resonance Solid-State Nuclear Magnetic Resonance”, Biochemistry, 54, 677-684 (2015) – highlighted on Biochemistry website.
P. Ratnayake, K. Sackett, M. J. Nethercott, and D. P. Weliky, “pH-Dependent Vesicle Fusion Induced by the Ectodomain of the Human Immunodeficiency Virus Membrane Fusion Protein gp41: Two Kinetically Distinct Processes and Fully-Membrane-Associated gp41 with Predominant β sheet Fusion Peptide Conformation”, Biochimica et Biophysica Acta, 1848, 289-298 (2015).
13. K. Banerjee and D. P. Weliky, “Folded Monomers and Hexamers of the Ectodomain of the HIV gp41 Membrane Fusion Protein: Potential Roles in Fusion and Synergy Between the Fusion Peptide, Hairpin, and Membrane-Proximal External Region”, Biochemistry, 53, 7184-7198 (2014).
K. Sackett, M. J. Nethercott, Z. Zheng, and D. P. Weliky, “Solid-State NMR Spectroscopy of the HIV gp41 Membrane Fusion Protein Supports Intermolecular Antiparallel b Sheet Fusion Peptide Structure in the Final Six-Helix Bundle State”, Journal of Molecular Biology, 426, 1077-1094 (2014).
15. C. M. Gabrys, W. Qiang, Y. Sun, L. Xie, S. D. Schmick, and D. P. Weliky, “Solid-State Nuclear Magnetic Resonance Measurements of HIV Fusion Peptide to Lipid 31P Proximities Support Similar Partially Inserted Membrane Locations of the a Helical and b Sheet Peptide Structures”, Journal of Physical Chemistry A, 117, 9848-9859 (2013).
16. E. P. Vogel and D. P. Weliky, “Quantitation of Recombinant Protein in Whole Cells and Cell Extracts via Solid-State NMR Spectroscopy”, Biochemistry, 52, 4285-4287 (2013) – highlighted on Biochemistry website.
17. U. Ghosh, L. Xie, and D. P. Weliky, “Detection of Closed Influenza Virus Hemagglutinin Fusion Peptide Structures in Membranes by Backbone 13CO-15N Rotational-Echo Double-Resonance Solid-State NMR”, Journal of Biomolecular NMR, 55, 139-146 (2013).
L. Xie, U. Ghosh, S. D. Schmick, and D. P. Weliky, “Residue-Specific Membrane Location of Peptides and Proteins Using Specifically and Extensively Deuterated Lipids and 13C-2H Rotational-Echo Double-Resonance Solid-State NMR”, Journal of Biomolecular NMR, 55, 11-17 (2013).
19. E. P. Vogel, J. Curtis-Fisk, K. M. Young, and D. P. Weliky, “Solid-State Nuclear Magnetic Resonance (NMR) Spectroscopy of Human Immunodeficiency Virus gp41 Protein that includes the Fusion Peptide: NMR Detection of Recombinant Fgp41 in Inclusion Bodies in Whole Bacterial Cells and NMR Structural Characterization of Purified and Membrane-Associated Fgp41”, Biochemistry, 50, 10013-10026 (2011).
20. K. Sackett, A. TerBush, and D. P. Weliky, “HIV Six-Helix Bundle Constructs Induce Rapid Vesicle Fusion at pH 3.5 and Little Fusion at pH 7.4: Understanding pH Dependence of Protein Aggregation, Membrane Binding, and Electrostatics, and Implications for HIV-Host Cell Fusion”, European Biophysics Journal, 40, 489-502 (2011).
21. S. D. Schmick and D. P. Weliky, “Major Antiparallel and Minor Parallel b Sheet Populations Detected in the Membrane-Associated Human Immunodeficiency Virus Fusion Peptide”, Biochemistry, 49, 10623-10635 (2010).
22. S. Tristram-Nagle, R. Chan, E. Kooijman, P. Uppamoochikkal, W. Qiang, D. P. Weliky, and J. F. Nagle, “HIV Fusion Peptide Penetrates, Disorders, and Softens T-cell Membrane Mimics”, Journal of Molecular Biology, 402, 139-153 (2010).
K. Sackett, M. J. Nethercott, R. F. Epand, R. M. Epand, D. R. Kindra, Y. Shai, and D. P. Weliky, “Comparative Analysis of Membrane-Associated Fusion Peptide Secondary Structure and Lipid Mixing Function of HIV gp41 Constructs that Model the Early Pre-Hairpin Intermediate and Final Hairpin Conformations”, Journal of Molecular Biology, 397, 301-315 (2010).
25. C. M. Gabrys, R. Yang, C. M. Wasniewski, J. Yang, C. G. Canlas, W. Qiang, Y. Sun, and D. P. Weliky, “Nuclear Magnetic Resonance Evidence for Retention of Lamellar Membrane Phase with Curvature in the Presence of Large Quantities of the HIV Fusion Peptide”, Biochimica et Biophysica Acta, 1798, 194-201 (2010).
N. Huarte, J. L. Nieva, S. Nir and D. P. Weliky, “Induced Perturbations and Adopted Conformations in Membranes by the HIV-1 Fusion Peptide”, In Membrane-Active Peptides: Methods and Results on Structure and Function, M. A. R. B. Castanho, Editor, International University Line:La Jolla, 2009, pp. 565-596.
27. I. Chung, J.-H. Song, M. G. Kim, C. D. Malliakas, A. L. Karst, A. J. Freeman, D. P. Weliky, and M. G. Kanatzidis, “The Tellurophosphate K4P8Te4: Phase-Change Properties, Exfoliation, Photoluminescence in Solution and Nanospheres”, Journal of the American Chemical Society, 131, 16303-16312 (2009).
Y. Sun and D. P. Weliky, “13C-13C Correlation Spectroscopy of Membrane-Associated Influenza Virus Fusion Peptide Strongly Supports a Helix-Turn-Helix Motif and Two Turn Conformations”, Journal of the American Chemical Society, 131, 13228-13229 (2009).
W. Qiang, Y. Sun, and D. P. Weliky, “A Strong Correlation Between Fusogenicity and Membrane Insertion Depth of the HIV Fusion Peptide”, Proceedings of the National Academy of Sciences of the U.S.A., 106, 15314-15319 (2009).
K. Sackett, M. J. Nethercott, Y. Shai, and D. P. Weliky, “Hairpin Folding of HIV gp41 Abrogates Lipid Mixing Function at Physiologic pH and Inhibits Lipid Mixing by Exposed gp41 Constructs”, Biochemistry, 48, 2714-2722 (2009).
W. Qiang and D. P. Weliky, “HIV Fusion Peptide and its Cross-Linked Oligomers: Efficient Syntheses, Significance of the Trimer in Fusion Activity, Correlation of b Strand Conformation with Membrane Cholesterol, and Proximity to Lipid Headgroups”, Biochemistry, 48, 289-301 (2009).
J. Curtis-Fisk, R. M. Spencer, and D. P. Weliky, “Native Conformation at Specific Residues in Recombinant Inclusion Body Protein in Whole Cells Determined with Solid-State Nuclear Magnetic Resonance Spectroscopy”, Journal of the American Chemical Society, 130, 12568-12569 (2008).
33. J. Curtis-Fisk, R. M. Spencer, and D. P. Weliky, “Isotopically Labeled Expression in E. coli, Purification, and Refolding of the Full Ectodomain of the Influenza Virus Membrane Fusion Protein”, Protein Expression and Purification, 61, 212-219 (2008).
W. Qiang, M. L Bodner, and D. P. Weliky, “Solid-State NMR Spectroscopy of HIV Fusion Peptides Associated with Host-Cell-Like Membranes: 2D Correlation Spectra and Distance Measurements Support a Fully Extended Conformation and Models for Specific Antiparallel Strand Registries”, Journal of the American Chemical Society, 130, 5459-5471 (2008).
35. M. A. Gave, K. M. Johnson, M. G. Kanatzidis, and D. P. Weliky, “Improved Resolution and Detection of 31P-Tl J-Couplings at 21 T in 31P Magic Angle Spinning Spectra of Inorganic Compounds Containing Tl/Bi/P/S”, Solid State Nuclear Magnetic Resonance, 33, 12-15 (2008).
M. L. Bodner, C. M. Gabrys, J. O. Struppe, and D. P. Weliky, “13C-13C and 15N-13C Correlation Spectroscopy of Membrane-Associated and Uniformly Labeled HIV and Influenza Fusion Peptides: Amino Acid-Type Assignments and Evidence for Multiple Conformations”, Journal of Chemical Physics, 128, 052319 (2008).
Z. Zheng, W. Qiang, and D. P. Weliky, “Investigation of Finite-Pulse Radiofrequency-Driven Recoupling Methods for Measurement of Intercarbonyl Distances in Polycrystalline and Membrane-Associated HIV Fusion Peptide Samples”, Magnetic Resonance in Chemistry, 45, S247-S260 (2007).
38. C. M. Gabrys and D. P. Weliky, “Chemical Shift Assignment and Structural Plasticity of a HIV Fusion Peptide Derivative in Dodecylphosphocholine Micelles”, Biochimica et Biophysica Acta-Biomembranes, 1768, 3225-3234 (2007).
40. I. Chung, J. I. Jang, M. A. Gave, D. P. Weliky, and M. G. Kanatzidis, “Low Valent Phosphorus in the Molecular Anions [P5Se12]5– and b-[P6Se12]4–: Phase Change Behavior and Near Infrared Second Harmonic Generation”, Chemical Communications, 4998-5000 (2007).
41. I. Chung, C. D. Malliakas, J. I. Jang, C. G. Canlas, D. P. Weliky, and M. G. Kanatzidis, “Helical Polymer 1/¥[P2Se62–]: Strong Second Harmonic Generation Response and Phase-Change Properties of its K and Rb Salts”, Journal of the American Chemical Society, 129, 14996-15006 (2007).
42. M. A. Gave, C. G. Canlas, I. Chung, R. G. Iyer, M. G. Kanatzidis, and D. P. Weliky, “Cs4P2Se10: A New Compound Discovered with the Application of Solid State and High Temperature NMR”, Journal of Solid State Chemistry, 180, 2877-2884 (2007).
43. J. Curtis-Fisk, C. Preston, Z. Zheng, R. M. Worden, and D. P. Weliky, “Solid-State NMR Structural Measurements on the Membrane-Associated Influenza Fusion Protein Ectodomain”, Journal of the American Chemical Society, 129, 11320-11321 (2007).
44. W. Qiang, J. Yang, and D. P. Weliky, “Solid-State Nuclear Magnetic Resonance Measurements of HIV Fusion Peptide to Lipid Distances Reveal the Intimate Contact of b Strand Peptide with Membranes and the Proximity of the Ala-14-Gly-16 Region with Lipid Headgroups”, Biochemistry, 46, 4997-5008 (2007).
M. A. Gave, C. D. Malliakas, D. P. Weliky, and M. G. Kanatzidis, “Wide Compositional and Structural Diversity in the System Tl/Bi/P/Q (Q = S, Se) and Observation of Vicinal P-Tl J Coupling in the Solid State”, Inorganic Chemistry, 46, 3632-3644 (2007).
46. Z. Zheng, R. Yang, M. L. Bodner, and D. P. Weliky, “Conformational Flexibility and Strand Arrangements of the Membrane-Associated HIV Fusion Peptide Trimer Probed by Solid-State NMR Spectroscopy”, Biochemistry, 45, 12960-12975 (2006).
48. O. Palchik, R. G. Iyer, C. G. Canlas, D. P. Weliky, and M. G. Kanatizidis, “K10M4M4¢S17 (M = Mn, Fe, Co, Zn; M¢ = Sn, Ge) and Cs10Cd4Sn4S17: Compounds with a Discrete Supertetrahedral Cluster”, Z. Anorg. Allg. Chem., 630, 2237-2247 (2004).
R. Yang, M. Prorok, F. J. Castellino, and D. P. Weliky, “A Trimeric HIV-1 Fusion Peptide Construct Which Does Not Self-Associate in Aqueous Solution and Which Has Fifteen-Fold Higher Membrane Fusion Rate”, Journal of the American Chemical Society, 126, 14722-14723 (2004).
C. M. Wasniewski, P. D. Parkanzky, M. L. Bodner, and D. P. Weliky, “Solid-State Nuclear Magnetic Resonance Studies of HIV and Influenza Fusion Peptide Orientations in Membrane Bilayers Using Stacked Glass Plate Samples”, Chemistry and Physics of Lipids, 132, 89-100 (2004).
52. I. Chung, J. Do, C. G. Canlas, D. P. Weliky, and M. G. Kanatizidis, “APSe6 (A = K, Rb, and Cs): Polymeric Selenophosphates with Reversible Phase-Change Properties”, Inorganic Chemistry, 43, 2762-2764 (2004).
53. M. L. Bodner, C. M. Gabrys, P. D. Parkanzky, J. Yang, C. A. Duskin, and D. P. Weliky, “Temperature Dependence and Resonance Assignment of 13C NMR Spectra of Selectively and Uniformly Labeled Fusion Peptides Associated with Membranes”, Magnetic Resonance in Chemistry, 42, 187-194 (2004).
54. J. Yang and D. P. Weliky, “Solid State Nuclear Magnetic Resonance Evidence for Parallel and Antiparallel Strand Arrangements in the Membrane-Associated HIV-1 Fusion Peptide”, Biochemistry, 42, 11879-11890 (2003).
55. R. J. DiCosty, D. P. Weliky, S. J. Anderson, and E. A. Paul, “15N-CPMAS Nuclear Magnetic Resonance Spectroscopy and Biological Stability of Soil Organic Nitrogen in Whole Soil and Particle-Size Fractions”, Organic Geochemistry, 34, 1635-1650 (2003).
56. C. G. Canlas, R. B. Muthukumaran, M. G. Kanatzidis, and D. P. Weliky, “Investigation of Longitudinal 31P Relaxation in Metal Selenophosphate Compounds”, Solid State Nuclear Magnetic Resonance, 24, 110-122 (2003).
57. C. G. Canlas, M. G. Kanatzidis, and D. P. Weliky, “31P Solid State NMR Studies of Metal Selenophosphates Containing [P2S6]4-, [P4S10]4-, [PSe4]3-, [P2Se7]4-, and [P2Se9]4- Ligands”, Inorganic Chemistry, 42, 3399-3405 (2003).
59. C. M. Gabrys, J. Yang, and D. P. Weliky, “Analysis of Local Conformation of Membrane-Bound and Polycrystalline Peptides by Two-Dimensional Slow-Spinning Rotor-Synchronized MAS Exchange Spectroscopy”, Journal of Biomolecular NMR, 26, 49-68 (2003).
60. J. Yang, P. D. Parkanzky, M. L. Bodner, C. G. Duskin, and D. P. Weliky, “Application of REDOR Subtraction for Filtered MAS Observation of Labeled Backbone Carbons of Membrane-Bound Fusion Peptides”, Journal of Magnetic Resonance, 159, 101–110 (2002).
61. K. K. Rangan, P. N. Trikalitis, C. Canlas, T. Bakas, D. P. Weliky, and M. G. Kanatzidis, “Hexagonal Pore Organization in Mesostructured Metal Tin Sulfides Built with [Sn2S6]4- Clusters”, Nano Letters, 2, 513 – 517 (2002).
63. J. Yang, C. M. Gabrys, and D. P. Weliky, “Solid State Nuclear Magnetic Resonance Evidence for an Extended b Strand Conformation of the Membrane-Bound HIV-1 Fusion Peptide”, Biochemistry, 40, 8126-8137 (2001).
64. J. Yang, P. D. Parkanzky, B. A. Khunte, C. G. Canlas, R. Yang, C. M. Gabrys, and D. P. Weliky, "Solid State NMR Measurements of Conformation and Conformational Distributions in the Membrane-Bound HIV-1 Fusion Peptide", Journal of Molecular Graphics and Modelling, 19, 129-135 (2001).
65. J. J. Balbach, J. Yang, D. P. Weliky, P. J. Steinbach, V. Tugarinov, J. Anglister, and R. Tycko, "Probing Hydrogen Bonds in the Antibody-Bound HIV-1 gp120 V3 Loop by Solid State NMR REDOR Measurements", Journal of Biomolecular NMR, 16, 313-327 (2000).
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