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<title>Chemistry and Biochemistry Faculty Publications</title>
<copyright>Copyright (c) 2013 Utah State University All rights reserved.</copyright>
<link>http://digitalcommons.usu.edu/chem_facpub</link>
<description>Recent documents in Chemistry and Biochemistry Faculty Publications</description>
<language>en-us</language>
<lastBuildDate>Wed, 06 Mar 2013 01:33:30 PST</lastBuildDate>
<ttl>3600</ttl>


	
		
	







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<title>Investigation of Antibacterial Mode of Action for Traditional and Amphiphilic Aminoglycosides</title>
<link>http://digitalcommons.usu.edu/chem_facpub/455</link>
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<pubDate>Mon, 04 Mar 2013 08:20:18 PST</pubDate>
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	<p>Aminoglycoside represents a class of versatile and broad spectrum antibacterial agents. In an effort to revive the antibacterial activity against aminoglycoside resistant bacteria, our laboratory has developed two new classes of aminoglycoside, pyranmycin and amphiphilic neomycin (NEOF004). The former resembles the traditional aminoglycoside, neomycin. The latter, albeit derived from neomycin, appears to exert antibacterial action via a different mode of action. In order to discern that these aminoglycoside derivatives have distinct antibacterial mode of action, RNA-binding affinity and fluorogenic dye were employed. These studies, together with our previous investigation, confirm that pyranmycin exhibit the traditional antibacterial mode of action of aminoglycosides by binding toward the bacterial rRNA. On the other hand, the amphiphilic neomycin, NEOF004 disrupts the bacterial cell wall. In a broader perspective, it verifies that structurally modified neomycin can exert different antibacterial mode of action leading to the revival of activity against aminoglycoside resistant bacteria.</p>

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<author>Venkatareddy Udumula et al.</author>


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<title>Phosphoryl and Sulfuryl Transfer</title>
<link>http://digitalcommons.usu.edu/chem_facpub/454</link>
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<pubDate>Tue, 02 Oct 2012 13:16:23 PDT</pubDate>
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<author>Tiago A.S. Brandão et al.</author>


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<title>Secondary Isotope Effects</title>
<link>http://digitalcommons.usu.edu/chem_facpub/453</link>
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<pubDate>Tue, 02 Oct 2012 13:16:22 PDT</pubDate>
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<author>Alvan C. Hengge</author>


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<title>Phosphoryl Transfer Reactions</title>
<link>http://digitalcommons.usu.edu/chem_facpub/452</link>
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<pubDate>Tue, 02 Oct 2012 13:16:21 PDT</pubDate>
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<author>Alvan C. Hengge</author>


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<title>Kinases</title>
<link>http://digitalcommons.usu.edu/chem_facpub/451</link>
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<pubDate>Tue, 02 Oct 2012 13:16:21 PDT</pubDate>
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<author>Alvan C. Hengge</author>


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<title>Phosphatases</title>
<link>http://digitalcommons.usu.edu/chem_facpub/450</link>
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<pubDate>Tue, 02 Oct 2012 13:16:20 PDT</pubDate>
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<author>Alvan C. Hengge</author>


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<title>Insights from Heavy-Atom Isotope Effects on Phosphoryl and Thiophosphoryl Transfer
Reactions</title>
<link>http://digitalcommons.usu.edu/chem_facpub/449</link>
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<pubDate>Tue, 02 Oct 2012 13:16:19 PDT</pubDate>
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<author>Alvan C. Hengge</author>


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<title>Transfer of the PO&lt;sub&gt;3&lt;/sub&gt;&lt;sup&gt;2-&lt;/sup&gt; Group</title>
<link>http://digitalcommons.usu.edu/chem_facpub/448</link>
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<pubDate>Tue, 02 Oct 2012 13:16:18 PDT</pubDate>
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<author>Alvan C. Hengge</author>


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<title>The molecular details of WPD-loop
movement differ in the protein-tyrosine phosphatases YopH and PTP1B</title>
<link>http://digitalcommons.usu.edu/chem_facpub/447</link>
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<pubDate>Tue, 02 Oct 2012 13:16:17 PDT</pubDate>
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<author>Tiago A.S. Brandão et al.</author>


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<title>Insights into the Phosphoryl
Transfer Mechanism of Cyclin-Dependent Protein Kinases from ab Initio QM/MM Free-Energy
Studies</title>
<link>http://digitalcommons.usu.edu/chem_facpub/446</link>
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<pubDate>Tue, 02 Oct 2012 13:16:17 PDT</pubDate>
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<author>Gregory K. Smith et al.</author>


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<title>The
Divalent Metal Ion in the Active Site of Uteroferrin Modulates Substrate Binding and Catalysis</title>
<link>http://digitalcommons.usu.edu/chem_facpub/445</link>
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<pubDate>Tue, 02 Oct 2012 13:16:16 PDT</pubDate>
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<author>Natasa Mitic et al.</author>


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<title>Insights into the Reaction of Proteintyrosine
Phosphatase 1B: Crystal Structures for Transition State Analogs of Both Catalytic Steps</title>
<link>http://digitalcommons.usu.edu/chem_facpub/444</link>
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<pubDate>Tue, 02 Oct 2012 13:16:14 PDT</pubDate>
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<author>Tiago A.S. Brandão et al.</author>


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<title>Active-Site Dynamics of SpvC Virulence Factor from Salmonella typhimurium and Density
Functional Theory Study of Phosphothreonine Lyase Catalysis</title>
<link>http://digitalcommons.usu.edu/chem_facpub/443</link>
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<pubDate>Tue, 02 Oct 2012 13:16:13 PDT</pubDate>
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<author>Gregory K. Smith et al.</author>


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<title>Mechanism and Transition State Structure of Aryl Methylphosphonate Esters Doubly Coordinated
to a Dinuclear Cobalt(III) Center</title>
<link>http://digitalcommons.usu.edu/chem_facpub/442</link>
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<pubDate>Tue, 02 Oct 2012 13:16:12 PDT</pubDate>
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<author>Guoqiang Feng et al.</author>


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<title>Impaired acid catalysis by
mutation of a protein loop hinge residue in a YopH mutant revealed by crystal structures</title>
<link>http://digitalcommons.usu.edu/chem_facpub/441</link>
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<pubDate>Tue, 02 Oct 2012 13:16:11 PDT</pubDate>
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<author>T. A.S. Brandão et al.</author>


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<title>An
Altered Transition State for the Reaction of an RNA Model Catalyzed by a Dinuclear Zinc(II)
Catalyst</title>
<link>http://digitalcommons.usu.edu/chem_facpub/440</link>
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<pubDate>Tue, 02 Oct 2012 13:16:10 PDT</pubDate>
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<author>T. Humphry et al.</author>


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<title>Substrate-Promoted
Formation of a Catalytically Competent Binuclear Center and Regulation of Reactivity in a
Glycerophosphodiesterase from Enterobacter aerogenes</title>
<link>http://digitalcommons.usu.edu/chem_facpub/439</link>
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<pubDate>Tue, 02 Oct 2012 13:16:09 PDT</pubDate>
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<author>K. S. Hadler et al.</author>


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<title>Mechanistic Study of Protein Phosphatase-1 (PP1), A Catalytically Promiscuous
Enzyme</title>
<link>http://digitalcommons.usu.edu/chem_facpub/438</link>
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<pubDate>Tue, 02 Oct 2012 13:16:08 PDT</pubDate>
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<author>C. McWhirter et al.</author>


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<title>The Effects of Sulfur Substitution for the Nucleophile and
Bridging Oxygen Atoms in Reactions of Hydroxyalkyl Phosphate Esters</title>
<link>http://digitalcommons.usu.edu/chem_facpub/437</link>
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<pubDate>Tue, 02 Oct 2012 13:16:07 PDT</pubDate>
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<author>Subashree Iyer et al.</author>


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<title>The Use of Isotopes in the Study of Reactions of Acyl, Phosphoryl,
and Sulfuryl Esters</title>
<link>http://digitalcommons.usu.edu/chem_facpub/436</link>
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<pubDate>Tue, 02 Oct 2012 13:16:06 PDT</pubDate>
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<author>R. H. Hoff et al.</author>


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