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  <title>NOPR Collection:</title>
  <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/19753" />
  <subtitle />
  <id>http://nopr.niscpr.res.in/handle/123456789/19753</id>
  <updated>2026-10-08T18:00:28Z</updated>
  <dc:date>2026-10-08T18:00:28Z</dc:date>
  <entry>
    <title>Identification of human proteins using the linguist's tools</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/19811" />
    <author>
      <name>Chattopadhyay, S</name>
    </author>
    <author>
      <name>Chakrabarti, J</name>
    </author>
    <author>
      <name>Bandyopadhyay, D</name>
    </author>
    <author>
      <name>Som, A</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/19811</id>
    <updated>2013-07-25T16:34:57Z</updated>
    <published>2001-04-01T00:00:00Z</published>
    <summary type="text">Title: Identification of human proteins using the linguist's tools
Authors: Chattopadhyay, S; Chakrabarti, J; Bandyopadhyay, D; Som, A
Abstract: The symbolic sequences of the exons that&#xD;
make human proteins are subjected to methods of statistical linguistics. The&#xD;
ideas developed for the natural languages by G. K. Zipf, when applied to these&#xD;
sequences, show significant promise. In particular, we argue, the Zipf's&#xD;
exponent differentiates, and hence, identifies disparate human sequences.
Page(s): 124-127</summary>
    <dc:date>2001-04-01T00:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Quantitative structure activity relationship (QSAR) studies of some substituted benzenesulphonyl glutamines as tumour suppressors</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/19810" />
    <author>
      <name>Srikanth, K</name>
    </author>
    <author>
      <name>Kumar, Ch. Anil</name>
    </author>
    <author>
      <name>Goswami, Diptendu</name>
    </author>
    <author>
      <name>De, A U</name>
    </author>
    <author>
      <name>Jha, Tarun</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/19810</id>
    <updated>2013-07-17T16:35:49Z</updated>
    <published>2001-04-01T00:00:00Z</published>
    <summary type="text">Title: Quantitative structure activity relationship (QSAR) studies of some substituted benzenesulphonyl glutamines as tumour suppressors
Authors: Srikanth, K; Kumar, Ch. Anil; Goswami, Diptendu; De, A U; Jha, Tarun
Abstract: As a part of a composite programme of rational&#xD;
drug design (RDD)&lt;sup&gt;1&lt;/sup&gt;, we had synthesized some substituted benzene&#xD;
sulphonyl glutamines and evaluated their inhibitory activities against Ehrlich&#xD;
Ascites Carcinoma (EAC) cell line in Swiss albino mice. Quantitative structure&#xD;
activity relationship (QSAR) studies of these inhibitory activities using&#xD;
Fujita-Ban&#xD;
&#xD;
model as well as Modified Hansch-Fujita&#xD;
model gave excellent correlations (correlation coefficient &lt;i&gt;r = &lt;/i&gt;0.89 and&#xD;
0.82 respectively). These results could be useful in designing 'lead' compound&#xD;
with potent inhibitory activity on DNA and RNA synthesis and tumour&#xD;
development.
Page(s): 120-123</summary>
    <dc:date>2001-04-01T00:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Wobble base-pairing in codon-anticodon interactions: A theoretical modelling study</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/19809" />
    <author>
      <name>Mangang, S Ulen</name>
    </author>
    <author>
      <name>Lyngdoh, R H Duncan</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/19809</id>
    <updated>2013-07-16T16:35:42Z</updated>
    <published>2001-04-01T00:00:00Z</published>
    <summary type="text">Title: Wobble base-pairing in codon-anticodon interactions: A theoretical modelling study
Authors: Mangang, S Ulen; Lyngdoh, R H Duncan
Abstract: The Crick wobble hypothesis attributes&#xD;
the phenomenon of codon degeneracy to a certain impreciseness of pairing between&#xD;
the third base of the codon and the first base of the anticodon. This&#xD;
theoretical study investigates the pairing properties of some wobble bases,&#xD;
including both, observed and unobserved pairs. Some wobble base-pairs are&#xD;
predicted to follow the Watson-Crick pairs in configuration and pairing&#xD;
facility, while others deviate from this norm. The observed U:V pair is unique&#xD;
in that a pairing configuration may be suggested for it wherein the&#xD;
hydrogen-bonding involves the exocyclic 5- carboxy methoxy group of V. By&#xD;
comparing the theoretical data on the configurations of these pairs with the&#xD;
evidence for&#xD;
&#xD;
their existence/non-existence in nature,&#xD;
some guidelines emerge for differentiating between observed and unobserved base&#xD;
pairs on the basis of the pairing configuration.
Page(s): 115-119</summary>
    <dc:date>2001-04-01T00:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Neural network prediction of 310-helices in proteins</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/19808" />
    <author>
      <name>Pal, Lipika</name>
    </author>
    <author>
      <name>Basu, Gautam</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/19808</id>
    <updated>2013-07-23T16:35:32Z</updated>
    <published>2001-04-01T00:00:00Z</published>
    <summary type="text">Title: Neural network prediction of 310-helices in proteins
Authors: Pal, Lipika; Basu, Gautam
Abstract: Secondary structure prediction from the&#xD;
primary sequence of a protein is fundamental to understanding its structure and&#xD;
folding properties. Although several prediction methodologies are in vogue,&#xD;
their performances are far from being completely satisfactory. Among these,&#xD;
non-linear neural networks have been shown to be relatively effective,&#xD;
especially for&#xD;
&#xD;
predicting -turns,&#xD;
where&#xD;
dominant interactions are local, arising from four sequence-contiguous&#xD;
residues. Most 3&lt;sub&gt;10&lt;/sub&gt;-helices in proteins arc also short comprising of&#xD;
three sequence-contiguous residues and two capping residues. In order to understand&#xD;
the extent of local interactions in these 3&lt;sub&gt;10&lt;/sub&gt;-helices, we have&#xD;
applied a neural network model with varying&#xD;
&#xD;
window size to predict 3&lt;sub&gt;10&lt;/sub&gt;-helices&#xD;
in proteins. We found the prediction accuracy of 3&lt;sub&gt;10&lt;/sub&gt;-helices (~ 14%),&#xD;
as judged by the Matthew's Correlation Coefficient, to be less than that of β-turns (~&#xD;
20%). The optimal window size for the prediction of 3&lt;sub&gt;10&lt;/sub&gt;-helices was&#xD;
about 9 residues. The significance and implications of these results in&#xD;
understanding the occurrence of 3&lt;sub&gt;10&lt;/sub&gt;-helices and preferences of amino&#xD;
acid residues in 3&lt;sub&gt;10&lt;/sub&gt;-helices are discussed.
Page(s): 107-114</summary>
    <dc:date>2001-04-01T00:00:00Z</dc:date>
  </entry>
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