Education Background

  • B.A. Chemistry and Computer Science DePauw University
  • Ph.D. Chemistry (1995)
    University of Michigan

Research Interests

  • Thiolate-rich Zn(II) sites and alkyl transfer: study of how the protein environment determines the reactivity of Zn(Cys) n(His) 4-n sites. Currently studying the Zn ribbon protein L36.
  • Designed protein motifs and carbon nanotubes: design of protein motifs that act to solubilize and organize single-walled carbon nanotubes into useful macromolecular structures.
  • DNA-binding domains: probe the molecular basis of gene regulation and DNA repair through the design of novel protein motifs that can bind specifically to particular portions of DNA, allowing us to control gene expression through binding or chemical modification.
  • Membrane fusion/protein-protein interactions: design of small protein domains that can bind to helical membrane fusion proteins and inhibit fusion as tools for studying protein-protein interactions, membrane fusion, and as possible antiviral agents against HIV, influenza, etc

Contact Information

Email: [email protected]
Phone: 972-883-2903
Fax: 972-883-2925
Office: BE2.522
Mail Stop: BE26
www.utdallas.edu/~dieckgr/


Gregg R. Dieckmann

The objectives of my research reflect my interests in inorganic chemistry, biochemistry and biophysics. Using an integrative approach, I plan to utilize protein design to create simple model systems that provide insights into the functioning of more complex biological systems.

One objective is to study biological membrane fusion, a process required for viral infection, intracellular transport and neurotransmitter release. Small protein domains that can bind to helical membrane fusion proteins and inhibit fusion will be designed as tools for studying membrane fusion, and as possible antiviral agents against HIV, influenza, etc.

Another research objective is to probe the molecular basis of gene regulation and DNA repair through the design of small protein domains that can bind specifically to particular portions of DNA, allowing us to control gene expression through binding or chemical modification. A third interest in the lab is the design of small metal-binding domains as models for naturally occuring metalloproteins.

Two specific targets include the metalloregulatory protein merR which binds mercury and is involved in heavy metal detoxification in bacteria, and the Zn-containing Ada demethylase, which repairs methylation damage in E. coli.

Selected Publications

Synthesis of Reversible Cyclic Peptides. Ortiz-Acevedo, A.; Dieckmann, G.R., Tet. Lett. (2004) 45(36): 6795-6798.

Hierarchical Self-Assembly of Peptide Coated Carbon Nanotubes. Dalton, A.B.; Ortiz-Acevedo, A.; Zorbas, V.; Sampson, W.M.; Collins, S.; Razal, J.; Yoshida, M.M.; Baughman, R.H.; Draper, R.K.; Musselman, I.H.; Jose-Yacaman, M.; Dieckmann, G.R., Adv. Funct. Mat. (2004) in press.

Preparation and Characterization of Individual Peptide-Wrapped Single-Walled Carbon Nanotubes. Zorbas, V.; Ortiz-Acevedo, A.; Dalton, A.B.; Yoshida, M.M.; Dieckmann, G.R.; Draper, R.K.; Baughman, R.H.; Jose-Yacaman, M.; Musselman, I.H. J. Am. Chem. Soc. (2004) 126: 7222-7227.

Solid Phase Synthesis of DOTA-Peptides. De Leon-Rodriguez, L.M.; Kovacs, Z.; Dieckmann, G.R.; Sherry, A.D., Chem. Eur. J. (2004) 10: 1149-1155.

Controlled Assembly of Carbon Nanotubes by Designed Amphiphilic Peptide Helices. Dieckmann, G.R.; Dalton, A.B.; Johnson, P.A.; Razal, J.; Chen, J.; Giordano, G.M.; Munoz, E.; Musselman, I.H.; Baughman, R.H.; Draper, R.K., J. Am. Chem. Soc. (2003) 125: 1770-1777.

Molecular Imprinting of Mesoporous SBA-15 with Chiral Ruthenium Complexes. Coutinho, D.; Ortiz-Acevedo, A.; Dieckmann, G.R.; Balkus Jr., K.J. Micropor. Mesopor. Mat. (2002) 54: 249.

Updated: November 30, 2005

©2005 The University of Texas at Dallas