Group Picture (Summer 2007)


Group Picture (Summer 2006)

 

Starring:

David Weliky as the faculty member – Weliky CV

Wei Qiang as a graduate research associate

Jaime Curtis as a graduate research associate

Yan Sun as a graduate research associate

Matthew Nethercott as a graduate research associate

Scott Schmick as a graduate research associate

Erica Schwander as a graduate research associate

Charles Gabrys as a postdoctoral associate

Kelly Sackett as a postdoctoral associate

 

FORMER GROUP MEMBERS

Matthew Gave (Ph. D. 2008, currently at scientist at Dow-Corning)

Zhaoxiong Zheng (Ph. D. 2007, currently a scientist in the Department of Pharmacology and Molecular Sciences at Johns Hopkins University)

Angela Karst (M. S. 2007, currently a scientist at American Litho)

Michele Bodner (Ph. D. 2006, currently a scientist at Varian, Inc.)

Paul Parkanzky (Ph. D. 2006, currently a scientist at Corium Corporation)

Rong Yang (Ph. D. 2005, currently a scientist at Bristol-Myers Squibb)

Christian Canlas (Ph. D. 2004, currently a research associate in the Department of Anesthesiology, University of Pittsburgh)

Jun Yang (Ph. D. 2003, currently a research associate in the Department of Molecular Cardiology, Lerner Research Institute, Cleveland Clinic)

Bhagyashree Khunte (M. S. 2001, currently a scientist at Pfizer Corporation)

 

POSTDOCTORAL POSITION

There are postdoctoral position(s) available in our laboratory for an NIH-funded project on solid state NMR studies of viral fusion peptides. These studies will provide insight into the mechanism of peptide-induced liposome fusion and ultimately, viral/host cell membrane fusion. The ideal applicant would have experience in modern solid state NMR and some experience in biochemistry, peptide synthesis, and/or protein expression. If you are interested, please email your c.v. and names of two references (with contact information) to Dr. David Weliky.  

 

 

Group Picture (2003)

 

Contact Information

Dr. Weliky telephone: 517-355-9715 ext. 281

Graduate Student/Post-doc telephone: 517-355-9715 ext. 282

Fax: 517-353-1793

Research

The Weliky group specializes in solid-state NMR spectroscopy with particular application to biological systems and to inorganic materials at high temperatures. 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 membrane-bound or fibrous proteins. We spend about 80% of our effort on applications and 20% of our effort on new methods development. Our research includes physical, analytical, organic, inorganic, and biological chemistries.

Applications

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 in frozen solution and membrane environments. 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 fusion protein. In addition, we are pursuing research on inorganic materials at high temperatures. 

New Methods

Fully Labeled Proteins: Our goal is to develop and apply new solid state NMR methods for resonance assignment and structure determination in these systems. This approach has the distinct advantage of requiring many fewer samples than is required when just a few nuclei are labeled.

 

Equipment

NMR

We have two 400 MHz Varian Chemagnetics Infinity Plus spectrometers. In addition, we have a variety of magic angle spinning and static probes. We also have time on a 900 MHz Bruker NMR at Michigan State University for which there are magic angle spinning and static probes. 

Biochemical

We have an ABI 431A peptide synthesizer, incubator shaker, refrigerated centrifuges, preparative HPLC, uv-vis spectrophotometer, and lyophilizer. We also have a nitrogen/vacuum line for organic derivatization of amino acids.

 

Publications (in pdf format)

1.                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).

2.                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).

3.                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).

4.                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).

5.                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).

6.                M. A. Gave, D. P. Weliky, and M. G. Kanatzidis, “New Potassium Bismuth Thiophosphates Including the Modulated K1.5Bi2.5(PS4)3”, Inorganic Chemistry, 46, 11063 -11074 (2007).

7.                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).

8.                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).

9.                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).

10.           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).

11.           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).

12.           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).

13.           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).

14.           I. Chung, A. L. Karst, D. P. Weliky, and M. G. Kanatzidis, “[P6Se12]4–: A Phosphorus-Rich Selenophosphate with Low-Valent P Centers”, Inorganic Chemistry, 45, 2785-2787 (2006).

15.           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).

16.           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).

17.           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).

18.           J. Yang, M. Prorok, F. J. Castellino, and D. P. Weliky, “Oligomeric Structure of the Membrane-Bound HIV-1 Fusion Peptide Formed From Soluble Monomers”, Biophysical Journal, 87, 1951-1963 (2004).

19.           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).

20.           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).

21.           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).

22.           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).

23.           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).

24.           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).

25.           R. Yang, J. Yang, and D. P. Weliky, “Synthesis, Enhanced Fusogenicity, and Solid State NMR Measurements of Cross-Linked HIV-1 Fusion Peptides”, Biochemistry, 42, 3527-3535 (2003).

26.           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).

27.           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).

28.           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).

29.           J. A. Aitken, C. Canlas, D. P. Weliky, and M. G. Kanatzidis, “[P2S10]4-: A Novel Polythiophosphate Anion Containing a Tetrasulfide Fragment”, Inorganic Chemistry, 40, 6496-6498 (2001).

30.           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).

31.           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).

32.           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).

 

Courses related to our work

Useful Scientific Links

National Magnetic Resonance Facility at Madison

Experimental Nuclear Magnetic Resonance Conference

National Institutes of Health Center for Research Resources

Center for Advanced Biotechnology and Medicine - Protein NMR Spectroscopy Laboratory

Learn or Teach NMR!

Michigan State University.

Michigan State University Department of Chemistry. This is the place where we all work to improve the world.

The Chemistry Department Brochure and Dr. Weliky’s brochure page.

The Protein Databank Page which stores information on the structure and composition of proteins and DNA fragments.

Software and Freeware

RasMol, a molecular display program.

Many of the pages here require Adobe Acrobat to view them properly. If you do not have Adobe Acrobat, please go here.
 
 

If you have comments or suggestions, email us at weliky@chemistry.msu.edu
 

This page created on June 5, 1998 and last modified on December 18, 2007!