Campus Directory: Hans-Joachim Wieden

University of Lethbridge

Hans-Joachim Wieden
Chemistry & Biochemistry
Office: E868 (University Hall)
Phone: (403) 329-2303


Postgraduate Training, Bioinformatics (Ruprecht-Karls-University, Heidelberg, Germany, 2003); Ph.D., Biochemistry (University of Witten/Herdecke, Germany, 2000); M.Sc., Chemistry (Heinrich-Heine University, Düsseldorf, Germany, 1995), B.Sc., Chemistry (Heinrich-Heine University, Düsseldorf, Germany, 1992)


Physical biochemistry, Rapid kinetics, Protein biosynthesis, Antibiotics, Ribosome function, Bioinformatics, Cryo-electron microscopy, Molecular modeling, RNA, Fluorescence spectroscopy, In vitro translation

Research Areas

Novel translation factors, Molecular dynamics of translation, Kinetics of translation, Antibiotic (mode of action), In vitro translation, assay development

Alternate Languages


Selected Publications

Dahl L. D., Wieden H.-J., Rodnina M. V., Knudsen C. R. (2006) The importance of P-loop and domain movements in EF-Tu for guanine nucleotide exchange.J. Biol. Chem. 281,21139-21146.

Buskiewicz I., Peske F., Wieden H.-J., Gryczynski I., Rodnina M. V., Wintermeyer W. (2005) Conformations of the Signal Recognition Particle Protein Ffh from Escherichia coli as Determined by FRET. J Mol Biol. 351,417-430.

Rodnina M.V., Gromadski K.B., Kothe U., Wieden H.-J. (2005) Recognition and selection of tRNA in translation. FEBS Lett. 579,938-942.

Kothe U., Wieden H.-J., Mohr D., Rodnina M.V. (2004) Interaction of helix D of elongation factor Tu with helices 4 and 5 of protein L7/12 on the ribosome. J Mol Biol. 336(5):1011-1021.

Daviter T, Wieden, H.-J., and Rodnina M. V. (2003) Essential role of histidine 84 in elongation factor Tu for the chemical step of GTP hydrolysis on the ribosome. J. Mol. Biol. 32,689-699.

Gu, S.-Q., Peske, F., Wieden, H.-J., Rodnina, M.V., and Wintermeyer, W. (2003) The signal recognition particle binds to protein L23 at the peptide exit of the E. coli ribosome. RNA 9, 566- 573.

Juranek, S., Wieden, H.-J, and Lipps, H. J. (2003) De novo cytosine methylation in the
differentiating macronucleus of the stichotrichous ciliate Stylonychia lemnae. Nuc. Acids Res. 31, 1387-1391.

Stark, H., Rodnina, M.V., Wieden, H.-J., Zemlin, F., Wintermeyer, W., and van Heel, M. (2002) Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon recognition complex. Nat. Struct. Biol. 9, 849-854.

Schirmer, J., Wieden, H.-J., Rodnina, M. V., and Aktories, K. (2002) Inactivation of the
elongation factor Tu by mosquitocidal toxin catalyzed mono-ADP-ribosylation. Appl. Environ. Microbiol. 68, 4894-4899.

Wieden, H.-J., Gromadski, K.B., Rodnin, D. N., and Rodnina, M. V. (2002) Mechanism of EF-Ts- catalzed nucleotide exchange in EF-Tu: Contribution of contacts at the guanine base. J. Biol. Chem. 277, 6032-6036.

Gromadski, K. B., Wieden, H.-J., and Rodnina, M. V. (2002) Kinetic mechanism of elongation factor Ts-catalyzed nucleotide exchange in elongation factor Tu. Biochemistry 41, 162-169.

Knudsen, C., Wieden, H.-J., and Rodnina, M. V. (2001) Importance of structural transitions of the switch II region for the functions of elongation factor Tu on the ribosome. J. Biol. Chem. 276, 22183-22190.

Wieden, H.-J., Wintermeyer, W. and Rodnina, M. V. (2001) A common structural motif in elongation factor Ts and ribosomal protein L7/12 may be involved in the interaction with
elongation factor Tu. J. Mol. Evol. 52, 129-136.

Stark, H., Rodnina, M.V., Wieden, H.-J., van Heel, M., and Wintermeyer, W. (2000) Large-scale movement of elongation factor G and extensive conformational changes of the ribosome during translocation. Cell 100, 301-309.

Rodnina, M. V., Stark, H., Savelsbergh, A., Wieden, H.-J., Mohr, D., Matassova, N. B., Peske, F., Daviter, T., Gualerzi, C. O., and Wintermeyer, W. (2000) GTPase mechanisms and functions of translation factors on the ribosome. Biol. Chem. 381, 377-387.

In The Media

An antibiotic Advisory: Dr. Hans-Joachim Wieden Says Antibiotics Are Too Widely Used; Legend; March 2007

How can we make antibiotics more effective? 2005-06 Community Report;

Wieden is the U of L's Sixth Canada Research Chair; Legend; December 2005

Research Interests

Structural and Functional dynamics of protein biosynthesis; the study of protein biosynthesis using a purified reconstituted E. coli translation system; kinetics and structural dynamics of elongation factors; functional roles of ribosomal proteins.

Current Research and Creative Activity

TitleLocationGrant InformationPrincipal InvestigatorCo Researchers
4 Dimensional molecular models for translation Lethbridge Alberta Ingenuity, $100,000 per annum, 2005-10.

H. Wieden, University of Lethbridge
Canada Research Chair in Physical Biochemistry Lethbridge Natural Sciences & Engineering Research Council (NSERC), $100,000 per annum.

H. Wieden, University of Lethbridge
Mechanism and Structural Dynamics of Translation Lethbridge Natural Sciences & Engineering Research Council (NSERC), $34,000 per annum, 2006-09.

Natural Sciences & Engineering Research Council (NSERC), $48,000, 2006-07.

H. Wieden, University of Lethbridge
Novel Mechanisms of Translation Inhibition Lethbridge Canadian Institutes of Health Research, Not funded, 2008-11.

H. Wieden, University of Lethbridge

Curriculum Vitae


Internet Links

The Wieden Team Pages

Edit this Content