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  <channel rdf:about="http://nopr.niscpr.res.in/handle/123456789/19759">
    <title>NOPR Collection:</title>
    <link>http://nopr.niscpr.res.in/handle/123456789/19759</link>
    <description />
    <items>
      <rdf:Seq>
        <rdf:li rdf:resource="http://nopr.niscpr.res.in/handle/123456789/19842" />
        <rdf:li rdf:resource="http://nopr.niscpr.res.in/handle/123456789/19841" />
        <rdf:li rdf:resource="http://nopr.niscpr.res.in/handle/123456789/19840" />
        <rdf:li rdf:resource="http://nopr.niscpr.res.in/handle/123456789/19839" />
      </rdf:Seq>
    </items>
    <dc:date>2026-10-09T14:20:26Z</dc:date>
  </channel>
  <item rdf:about="http://nopr.niscpr.res.in/handle/123456789/19842">
    <title>A new form of Scatchard plot to study binding of fluoride ion on urease by isothermal titration calorimetry</title>
    <link>http://nopr.niscpr.res.in/handle/123456789/19842</link>
    <description>Title: A new form of Scatchard plot to study binding of fluoride ion on urease by isothermal titration calorimetry
Authors: Saboury, A A
Abstract: A new equation with a useful simple graphical&#xD;
method, very similar to the Scatchard plot was introduced to obtain the equilibrium&#xD;
constant and the enthalpy of binding using isothermal titration calorimetric&#xD;
data. On applying this simple graphical method to study the binding of fluoride&#xD;
ion on jack bean urease, the dissociation equilibrium constant obtained was remarkably&#xD;
consistent with the inhibition constant obtained from assay of enzyme activity in&#xD;
the presence of fluoride ion.
Page(s): 347-350</description>
    <dc:date>2000-10-01T00:00:00Z</dc:date>
  </item>
  <item rdf:about="http://nopr.niscpr.res.in/handle/123456789/19841">
    <title>Adsorption of glycine and alanine on montmorillonite with or without coordinated divalent cations</title>
    <link>http://nopr.niscpr.res.in/handle/123456789/19841</link>
    <description>Title: Adsorption of glycine and alanine on montmorillonite with or without coordinated divalent cations
Authors: Kalra, Sippy; Pant, C K; Pathak, H D; Mehta, M S
Abstract: Adsorption of glycine and alanine on montmorillonite&#xD;
and on Ca&lt;sup&gt;2+&lt;/sup&gt;- and Mg&lt;sup&gt;2+&lt;/sup&gt;- exchanged montmorillonite clay&#xD;
over a range of &lt;i&gt;p&lt;/i&gt;H (4.0-9.0) and temperature (20-35&lt;sup&gt;o&lt;/sup&gt;C) under possible&#xD;
abiotic conditions have been investigated UV-spectrophotometrically. Adsorption&#xD;
of both the amino acids was considerable on all the three adsorbents used.&#xD;
Maximum adsorption was observed at 25&lt;sup&gt;o&lt;/sup&gt; C and neutral &lt;i&gt;p&lt;/i&gt;H. Ca&lt;sup&gt;2+&lt;/sup&gt;-montmorillonite&#xD;
exhibited relatively better adsorption as compared to Mg&lt;sup&gt;2+&lt;/sup&gt;-exchanged&#xD;
form or montmorillonite. The values of K&lt;sub&gt;L&lt;/sub&gt; and X&lt;sub&gt;m&lt;/sub&gt; were&#xD;
determined using Langmuir isotherm characteristics.
Page(s): 341-346</description>
    <dc:date>2000-10-01T00:00:00Z</dc:date>
  </item>
  <item rdf:about="http://nopr.niscpr.res.in/handle/123456789/19840">
    <title>X -band EPR spectra of copper(II)-dipeptide-imlidazole (1:1:0/1) system</title>
    <link>http://nopr.niscpr.res.in/handle/123456789/19840</link>
    <description>Title: X -band EPR spectra of copper(II)-dipeptide-imlidazole (1:1:0/1) system
Authors: Patel, R N; Pandeya, K B
Abstract: The electron paramagnetic resonance (EPR)&#xD;
spectra of copper(II)-GA/GV and copper(II)-GA/GV-imH/eimH/ m-imH have been recorded&#xD;
as a function of &lt;i&gt;p&lt;/i&gt;H&lt;i&gt;. &lt;/i&gt;Imidazole enters coordination at &lt;i&gt;p&lt;/i&gt;H ~&#xD;
7.0, whereas the substituted imidazoles do so at &lt;i&gt;p&lt;/i&gt;H&gt; 7.0. The σ-bonding&#xD;
appears to have a moderate degree of covalency. In-plane and out-of-plane π-bonding&#xD;
has been found to be more strongly covalent.
Page(s): 334-340</description>
    <dc:date>2000-10-01T00:00:00Z</dc:date>
  </item>
  <item rdf:about="http://nopr.niscpr.res.in/handle/123456789/19839">
    <title>Synthesis, conformation and vibrational dynamics of apolipoprotein B fragment, -Asn-Cys-Lys-Val-Glu-Leu-</title>
    <link>http://nopr.niscpr.res.in/handle/123456789/19839</link>
    <description>Title: Synthesis, conformation and vibrational dynamics of apolipoprotein B fragment, -Asn-Cys-Lys-Val-Glu-Leu-
Authors: Srivastava, Seema; Melkani, Girish Chandra; Singh, Shyam; Gupta, Vishwambhar Dayal
Abstract: It is assumed that all biological processes&#xD;
are dynamical in nature and the low frequency collective modes, particularly the&#xD;
skeletal modes arising from the main chain and the side chain play an important&#xD;
role in such processes. To identify these a complete normal mode analysis of the&#xD;
hexapeptide -Asn-Cys-Lys-Yal-Glu-Leu-, a&#xD;
fragment of apolipoprotein B has been carried out. The assignment of modes is greatly&#xD;
assisted by similar studies on the tetra -Cys-Lys-Val-Glu- and tripeptides (-Asn-Cys-Lys-, -Yal-Glu-Leu-) fragments of the hexapeptide. All the&#xD;
four peptides have been synthesized by the solid phase peptide method using 9-flurrenyl&#xD;
methyloxycarbonyl (Fmoc) on 4-methyl benzhyldrylamine (MBHA) and Wang's resins.&#xD;
Their conformation is determined from the Ramachandran Maps which are based on the&#xD;
global energy minimization method. It is supported by the propensity parameters&#xD;
for the amino acids.
Page(s): 318-333</description>
    <dc:date>2000-10-01T00:00:00Z</dc:date>
  </item>
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