Browsing University Archives by Author "Wieden, Hans-Joachim"

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  • Characterization of the universally conserved ATPase YchF using an in vitro and in silico approach 
    Rosler, Kirsten S; University of Lethbridge. Faculty of Arts and Science (Lethbridge, Alta : University of Lethbridge, Dept. of Chemistry and BiochemistryFaculty of Arts and ScienceDepartment of Chemistry and Biochemistry, 2014)
    GTPases perform a myriad of functions within the cell, from protein synthesis to cellular signaling. Of all known GTPases, only eight are conserved across all three domains of life. YchF is one of the eight universally ...
  • Functional role of the conserved amino acids Cysteine 81, Arginine 279, Glycine 280 and Arginine 283 in elongation factor Tu from Escherichia coli 
    Mo, Fan (Lethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistry, c2011Arts and ScienceDepartment of Chemistry and Biochemistry, 2011)
    During protein synthesis, elongation factor Tu (EF-Tu) delivers aminoacyl-tRNA (aa-tRNA) to the A-site of mRNA-programmed ribosomes in a GTP-dependent manner. To enable future studies on the functional and structural ...
  • Initial characterization of the ribosome-associated ATP binding cassette (ABC) protein YHIH from E. Coli 
    Fischer, Jeffrey J.; University of Lethbridge. Faculty of Arts and Science (Lethbridge, Alta. : University of Lethbridge, Faculty of Arts and Science, 2007Arts and ScienceDepartment of Chemistry and Biochemistry, 2007)
    Protein synthesis is a highly conserved process across all domains of life, both structurally and functionally. This cyclic process is catalyzed by numerous soluble protein factors that interact with the ribosome to ...
  • Insight into the universally conserved NTPases HflX and YchF 
    Coatham, Mackenzie Leigh (Lethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and BiochemistryArts and ScienceDepartment of Chemistry and Biochemistry, 2014)
    The functional roles of the two universally conserved bacterial GTPases, HflX and YchF, are poorly understood. Both proteins associate with 70S ribosomes as well as 30S and 50S ribosomal subunits. Understanding exactly how ...
  • Kinetic analyses on two translational GTPases : LepA and EF-Tu 
    De Laurentiis, Evelina Ines (Lethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and BiochemistryArts and ScienceDepartment of Chemistry and Biochemistry, 2013)
    Protein synthesis is an essential process for all living organisms and is an effective major target for current antibiotics. Elongation factor Tu (EF-Tu) is a highly conserved and essential protein that functions during ...
  • Rapid kinetic studies of PhyA from Selenomonas ruminantium, and a simplified means of production of a phosphate biosensor 
    Smith, Dustin D.; University of Lethbridge. Faculty of Arts and Science (Lethbridge, Alta : University of Lethbridge, Dept. of Chemistry and BiochemistryArts and ScienceDepartment of Biological SciencesDepartment of Chemistry and Biochemistry, 2016)
    Myo-inositol polyphosphates (IPs) are ubiquitous in nature and involved in various cellular events. Dephosphorylation of IPs by protein tyrosine phosphatase-like polyphosphatases (PTPLPs) occurs via a complex pathway, and ...
  • The role of tetracycline and macromolecular crowding on the function of elongation factor-Tu 
    Gzyl, Katherine Elizabeth; University of Lethbridge. Faculty of Arts and Science (Lethbridge, Alta. : Universtiy of Lethbridge, Department of Chemistry and BiochemistryArts and ScienceDepartment of Chemistry and Biochemistry, 2017)
    The cellular environment affects dynamics of proteins moving from one conformation into another. Aspects of the cellular environment such as availability of ligands, osmolytes, and antibiotics affect proteins. However, ...
  • Structural and functional dynamics of Escherichia coli ribonuclease II : initial studies using a novel fluorescence based system 
    Smith, Adam David; University of Lethbridge. Faculty of Arts and Science (Lethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistry, c2009Arts and ScienceDepartment of Chemistry and Biology, 2009)
    Ribonuclease II (RNase II) is a bacterial enzyme responsible for 90% of the ...
  • Structural dynamics of elongation factor Tu 
    Mercier, Evan A. (Lethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and BiochemistryArts and ScienceDepartment of Chemistry and Biochemistry, 2013)
    Elongation Factor (EF) Tu is universally conserved and delivers aminoacyl-tRNAs (aatRNAs) to the ribosome. To perform this essential task, EF-Tu binds aa-tRNA in an active GTP-bound state, and GTP hydrolysis is critical ...
  • Toward understanding the function of the universally conserved GTPase HflX 
    Fischer, Jeffrey J. (Lethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistry, c2011Arts and ScienceDepartment of Chemistry and Biochemistry, 2011)
    Members of the ubiquitous GTPase superfamily regulate numerous cellular functions. A core group of eight GTPases are present in all domains of life: initiation factor 2, elongation factors Tu and G, protein secretion factors ...
  • Two partners of the ribosome, EF-Tu and LepA 
    de Laurentiis, Evelina Ines; University of Lethbridge. Faculty of Arts and Science (Lethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistry, c2009Arts and ScienceDepartment of Chemistry and Biochemistry, 2009)
    The translational GTPases elongation factor Tu (EF-Tu) and LepA modulate the dynamics of tRNA on the ribosome. EF-Tu facilitates the delivery of aminoacyl-tRNA (aa-tRNA) to the translating ribosome and LepA catalyzes the ...

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