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<title>Volume 10, Issue 3 (2014) | American Journal of Biochemistry and Biotechnology</title>
<description>Volume 10, Issue 3 (2014) | American Journal of Biochemistry and Biotechnology</description>
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    <title><![CDATA[Structural Characterization at the Atomic Level of a Molecular Nano-Machine: The State of the Art of <i>Helicobacter Pylori</i> Flagellum Organization]]></title>
    <link>https://thescipub.com/ajbb/ajbbsp.2014.143.161</link>
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        <![CDATA[<p>American Journal of Biochemistry and Biotechnology, Published online: 12 November 2014; <a href="https://thescipub.com/ajbb/ajbbsp.2014.143.161">doi:10.3844/ajbbsp.2014.143.161</a></p>Motility is fundamental for success in colonization and survival of the human pathogen H. pylori, the bacterium that colonizes about half of the human population. Motility is achieved through flagella...]]></content:encoded>
    <dc:title><![CDATA[Structural Characterization at the Atomic Level of a Molecular Nano-Machine: The State of the Art of <i>Helicobacter Pylori</i> Flagellum Organization]]></dc:title><dc:creator>Ivana  Pulić</dc:creator><dc:creator>Valentina  Loconte</dc:creator><dc:creator>Giuseppe  Zanotti</dc:creator><dc:identifier>doi:10.3844/ajbbsp.2014.143.161</dc:identifier>
    <dc:source>American Journal of Biochemistry and Biotechnology, Published online: 2014-11-12; | doi:10.3844/ajbbsp.2014.143.161</dc:source>
    <dc:date>2014-11-12</dc:date>
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    <prism:doi>10.3844/ajbbsp.2014.143.161</prism:doi>
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    </item><item rdf:about="https://thescipub.com/ajbb/ajbbsp.2014.162.168">
    <title><![CDATA[Synchrotron Powder Diffraction Study of Radiation Damage in Langmuir Blodgett Nanotemplate Crystallised Protein]]></title>
    <link>https://thescipub.com/ajbb/ajbbsp.2014.162.168</link>
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        <![CDATA[<p>American Journal of Biochemistry and Biotechnology, Published online: 12 November 2014; <a href="https://thescipub.com/ajbb/ajbbsp.2014.162.168">doi:10.3844/ajbbsp.2014.162.168</a></p>Polycrystalline samples of lysozyme were prepared with and without a Langmuir-Blodgett (LB) thin film template via both the hanging drop method and batch crystallisation. Powder diffraction methods ar...]]></content:encoded>
    <dc:title><![CDATA[Synchrotron Powder Diffraction Study of Radiation Damage in Langmuir Blodgett Nanotemplate Crystallised Protein]]></dc:title><dc:creator>Jonathan P. Wright</dc:creator><dc:creator>Eugenia  Pechkova</dc:creator><dc:creator>Claudio  Nicolini</dc:creator><dc:identifier>doi:10.3844/ajbbsp.2014.162.168</dc:identifier>
    <dc:source>American Journal of Biochemistry and Biotechnology, Published online: 2014-11-12; | doi:10.3844/ajbbsp.2014.162.168</dc:source>
    <dc:date>2014-11-12</dc:date>
    <prism:publicationName>Science Publications</prism:publicationName>
    <prism:doi>10.3844/ajbbsp.2014.162.168</prism:doi>
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    </item><item rdf:about="https://thescipub.com/ajbb/ajbbsp.2014.169.179">
    <title><![CDATA[Probing the Substrate Specificity and Intersubunit Interactions of <i>Brevundimonas Diminuta</i> Glutaryl Acylase with Site-Directed Mutagenesis]]></title>
    <link>https://thescipub.com/ajbb/ajbbsp.2014.169.179</link>
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        <![CDATA[<p>American Journal of Biochemistry and Biotechnology, Published online: 12 November 2014; <a href="https://thescipub.com/ajbb/ajbbsp.2014.169.179">doi:10.3844/ajbbsp.2014.169.179</a></p>Glutaryl-7-ACA acylases (GLA) are industrial enzymes widely used for the production of 7-aminocepahlosporanic acid (7-ACA)-the starting compound for manufacturing of semisynthetic cephalosporin antibi...]]></content:encoded>
    <dc:title><![CDATA[Probing the Substrate Specificity and Intersubunit Interactions of <i>Brevundimonas Diminuta</i> Glutaryl Acylase with Site-Directed Mutagenesis]]></dc:title><dc:creator>Michael  Eldarov</dc:creator><dc:creator>Anna  Lyashenko</dc:creator><dc:creator>Tatyana  Sherbakova</dc:creator><dc:creator>Dmitry  Suplatov</dc:creator><dc:creator>  KirillKopylov</dc:creator><dc:creator>Vytas  Svedas</dc:creator><dc:identifier>doi:10.3844/ajbbsp.2014.169.179</dc:identifier>
    <dc:source>American Journal of Biochemistry and Biotechnology, Published online: 2014-11-12; | doi:10.3844/ajbbsp.2014.169.179</dc:source>
    <dc:date>2014-11-12</dc:date>
    <prism:publicationName>Science Publications</prism:publicationName>
    <prism:doi>10.3844/ajbbsp.2014.169.179</prism:doi>
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    </item><item rdf:about="https://thescipub.com/ajbb/ajbbsp.2014.180.188">
    <title><![CDATA[Docking and Molecular Dynamics Simulations in Potential Drugs Discovery: An Application to Influenza Virus M2 Protein]]></title>
    <link>https://thescipub.com/ajbb/ajbbsp.2014.180.188</link>
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        <![CDATA[<p>American Journal of Biochemistry and Biotechnology, Published online: 11 November 2014; <a href="https://thescipub.com/ajbb/ajbbsp.2014.180.188">doi:10.3844/ajbbsp.2014.180.188</a></p>Molecular docking is a common method for searching new potential drugs. Improvement of the results of docking can be achieved by different ways-one of them is molecular dynamics simulations of protein...]]></content:encoded>
    <dc:title><![CDATA[Docking and Molecular Dynamics Simulations in Potential Drugs Discovery: An Application to Influenza Virus M2 Protein]]></dc:title><dc:creator>Marine E. Bozdaganyan</dc:creator><dc:creator>Philipp S. Orekhov</dc:creator><dc:creator>Nicola L. Bragazzi</dc:creator><dc:creator>Donatella  Panatto</dc:creator><dc:creator>Daniela  Amicizia</dc:creator><dc:creator>Eugenia  Pechkova</dc:creator><dc:creator>Claudio  Nicolini</dc:creator><dc:creator>Roberto  Gasparini</dc:creator><dc:identifier>doi:10.3844/ajbbsp.2014.180.188</dc:identifier>
    <dc:source>American Journal of Biochemistry and Biotechnology, Published online: 2014-11-11; | doi:10.3844/ajbbsp.2014.180.188</dc:source>
    <dc:date>2014-11-11</dc:date>
    <prism:publicationName>Science Publications</prism:publicationName>
    <prism:doi>10.3844/ajbbsp.2014.180.188</prism:doi>
    <prism:url>https://thescipub.com/ajbb/ajbbsp.2014.180.188</prism:url>
    </item><item rdf:about="https://thescipub.com/ajbb/ajbbsp.2014.189.201">
    <title><![CDATA[Drug-Protein Interactions for Clinical Research by Nucleic Acid Programmable Protein Arrays-Quartz Crystal Microbalance with Dissipation Factor Monitoring Nanoconductometric Assay]]></title>
    <link>https://thescipub.com/ajbb/ajbbsp.2014.189.201</link>
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        <![CDATA[<p>American Journal of Biochemistry and Biotechnology, Published online: 17 November 2014; <a href="https://thescipub.com/ajbb/ajbbsp.2014.189.201">doi:10.3844/ajbbsp.2014.189.201</a></p>Conductometric monitoring of drug-gene and drug-protein interactions is of fundamental importance in the field of molecular pharmacology. Here, we present our main findings and characterizations of an...]]></content:encoded>
    <dc:title><![CDATA[Drug-Protein Interactions for Clinical Research by Nucleic Acid Programmable Protein Arrays-Quartz Crystal Microbalance with Dissipation Factor Monitoring Nanoconductometric Assay]]></dc:title><dc:creator>Claudio  Nicolini</dc:creator><dc:creator>Rosanna  Spera</dc:creator><dc:creator>Nicola Luigi Bragazzi</dc:creator><dc:creator>Eugenia  Pechkova</dc:creator><dc:identifier>doi:10.3844/ajbbsp.2014.189.201</dc:identifier>
    <dc:source>American Journal of Biochemistry and Biotechnology, Published online: 2014-11-17; | doi:10.3844/ajbbsp.2014.189.201</dc:source>
    <dc:date>2014-11-17</dc:date>
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    <prism:doi>10.3844/ajbbsp.2014.189.201</prism:doi>
    <prism:url>https://thescipub.com/ajbb/ajbbsp.2014.189.201</prism:url>
    </item><item rdf:about="https://thescipub.com/ajbb/ajbbsp.2014.202.207">
    <title><![CDATA[Raman Spectroscopy of Protein Crystal Nucleation and Growth]]></title>
    <link>https://thescipub.com/ajbb/ajbbsp.2014.202.207</link>
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        <![CDATA[<p>American Journal of Biochemistry and Biotechnology, Published online: 8 December 2014; <a href="https://thescipub.com/ajbb/ajbbsp.2014.202.207">doi:10.3844/ajbbsp.2014.202.207</a></p>Using Raman spectroscopy and the lysozyme as model system, we investigate the differences in protein conformation before and after Langmuir-Blodgett nanotemplate-induced crystal nucleation and growth....]]></content:encoded>
    <dc:title><![CDATA[Raman Spectroscopy of Protein Crystal Nucleation and Growth]]></dc:title><dc:creator>Pechkova  Eugenia</dc:creator><dc:creator>  Maksimov</dc:creator><dc:creator>  Georgy</dc:creator><dc:creator>Parshina  Evgenia</dc:creator><dc:creator>Maksimov  Evgenii</dc:creator><dc:creator>Kutusov  Nikolai</dc:creator><dc:creator>Brazhe  Nadezda</dc:creator><dc:creator>Tarasova  Irina</dc:creator><dc:creator>Stefano  Fiordoro</dc:creator><dc:creator>Nicolini  Claudio</dc:creator><dc:identifier>doi:10.3844/ajbbsp.2014.202.207</dc:identifier>
    <dc:source>American Journal of Biochemistry and Biotechnology, Published online: 2014-12-08; | doi:10.3844/ajbbsp.2014.202.207</dc:source>
    <dc:date>2014-12-08</dc:date>
    <prism:publicationName>Science Publications</prism:publicationName>
    <prism:doi>10.3844/ajbbsp.2014.202.207</prism:doi>
    <prism:url>https://thescipub.com/ajbb/ajbbsp.2014.202.207</prism:url>
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