<?xml version="1.0" encoding="UTF-8"?>
<article article-type="research-article" xml:lang="en" xmlns:xlink="http://www.w3.org/1999/xlink">
<front>
<journal-meta>
<journal-id journal-id-type="publisher">global-journal-of-science-frontier-research-a-physics-space-science</journal-id>
<journal-title-group>
<journal-title>Global Journal of Science Frontier Research - A: Physics &amp; Space Science</journal-title>
</journal-title-group>
<issn publication-format="print">0975-5896</issn>
<issn publication-format="electronic">2249-4626</issn>
<publisher><publisher-name>Global Journals Publishing Group Incorporated</publisher-name></publisher>
<self-uri xlink:href="https://globaljournals.org/journal-seo-export/jats/52662.xml" />
</journal-meta>
<article-meta>
<article-id pub-id-type="publisher-id">52662</article-id>
<title-group>
<article-title>Inspection of Remodeling Impacts of Domain Movements in Hydrosoluble Protein Using Dual Artificial Intelligence Methods</article-title>
<subtitle>Remodeling Domain Movements in Ficin Proteins</subtitle>
</title-group>
<contrib-group>
<contrib contrib-type="author"><name><surname>Nishiyama</surname><given-names>Katsuhiko</given-names></name><xref ref-type="aff" rid="aff1" />
</contrib>
</contrib-group>
<aff id="aff1">JAPAN, National Institute of Technology (KOSEN), Ishikawa College</aff>
<pub-date publication-format="electronic" date-type="pub" iso-8601-date="2022-06-15">
<day>15</day>
<month>06</month>
<year>2022</year>
</pub-date>
<volume>22</volume>
<issue>A3</issue>
<fpage>3</fpage>
<lpage>15</lpage>
<abstract><p>Remodeling impacts of domain movements in protease are of interest in many fields such as medical treatments, food processing, and bio-electronic devices. However, they are yet to be precisely explained. In this study, the remodeling effects in ficin were investigated via a deep neural network, genetic programming, and computer simulations. The replacement (Y113F) in ficin using domain movements exhibited a critical effect on the peptide compatibilities. Specifically, modification of amino acid allows the remodeling of the domain movements, and types of compatible peptides should be modulated by the remodeling. Moreover, the decision tree revealed important factors in peptides and ficin.</p></abstract>
<kwd-group kwd-group-type="author-generated">
<kwd>protein</kwd>
<kwd>deep neural networks</kwd>
<kwd>genetic programming</kwd>
<kwd>molecular dynamics simulations.</kwd>
</kwd-group>
<self-uri content-type="pdf" xlink:href="https://globaljournals.org/GJSFR_Volume22/2-Inspection-of-Remodeling.pdf" />
<self-uri content-type="html" xlink:href="https://globaljournals.org/scholarly-articles/inspection-of-remodeling-impacts-of-domain-movements-in-hydrosoluble-protein-using-dual-artificial-intelligence-methods/" />
</article-meta>
</front>
<body>
<sec>
<title>Full Text</title>
<p>Remodeling impacts of domain movements in protease are of interest in many fields such as medical treatments, food processing, and bio-electronic devices. However, they are yet to be precisely explained. In this study, the remodeling effects in ficin were investigated via a deep neural network, genetic programming, and computer simulations. The replacement (Y113F) in ficin using domain movements exhibited a critical effect on the peptide compatibilities. Specifically, modification of amino acid allows the remodeling of the domain movements, and types of compatible peptides should be modulated by the remodeling. Moreover, the decision tree revealed important factors in peptides and ficin.</p>
</sec>
</body>
</article>