<?xml version="1.0" encoding="ISO-8859-1"?><article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance">
<front>
<journal-meta>
<journal-id>0035-001X</journal-id>
<journal-title><![CDATA[Revista mexicana de física]]></journal-title>
<abbrev-journal-title><![CDATA[Rev. mex. fis.]]></abbrev-journal-title>
<issn>0035-001X</issn>
<publisher>
<publisher-name><![CDATA[Sociedad Mexicana de Física]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S0035-001X2023000300022</article-id>
<article-id pub-id-type="doi">10.31349/revmexfis.69.031701</article-id>
<title-group>
<article-title xml:lang="es"><![CDATA[Dinámica molecular de grano grueso de la proteína tau]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Robert-Jiménez]]></surname>
<given-names><![CDATA[L.]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Figueroa-Gerstenmaier]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Basurto-Islas]]></surname>
<given-names><![CDATA[G.]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Herrera-Velarde]]></surname>
<given-names><![CDATA[S.]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Instituto Tecnológico Superior de Xalapa Tecnológico Nacional de México Subdirección de Posgrado e Investigación]]></institution>
<addr-line><![CDATA[Xalapa Veracruz]]></addr-line>
<country>Mexico</country>
</aff>
<aff id="Af2">
<institution><![CDATA[,Universidad de Guanajuato Campus León Departamento de Ingenierías Química, Electrónica y Biomédica]]></institution>
<addr-line><![CDATA[León Guanajuato]]></addr-line>
<country>Mexico</country>
</aff>
<aff id="Af3">
<institution><![CDATA[,Instituto Tecnológico Superior de Xalapa Tecnológico Nacional de México Subdirección de Posgrado e Investigación]]></institution>
<addr-line><![CDATA[Xalapa Veracruz]]></addr-line>
<country>Mexico</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>06</month>
<year>2023</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>06</month>
<year>2023</year>
</pub-date>
<volume>69</volume>
<numero>3</numero>
<fpage>0</fpage>
<lpage>0</lpage>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_arttext&amp;pid=S0035-001X2023000300022&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_abstract&amp;pid=S0035-001X2023000300022&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_pdf&amp;pid=S0035-001X2023000300022&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="es"><p><![CDATA[Resumen Actualmente, a nivel mundial, alrededor de 48 millones de personas padecen la enfermedad de Alzheimer, la forma más común de demencia, para la cual no hay cura. La enfermedad se debe, parcialmente, a las alteraciones postraduccionales que experimenta la proteína tau y que favorecen su polimerización anormal formando fibrillas y marañas neurofibrilares. La tau es una proteína intrínsecamente desordenada, es decir, no posee una estructura bien definida. Una técnica eficaz en el estudio de este tipo de proteínas es la dinámica molecular. En este trabajo se utilizó esta técnica empleando el campo de fuerza SIRAH (del inglés: Southamerican Initiative for a Rapid and Accurate Hamiltonian) para modelar dos sistemas distintos de tau, cada uno con dos moléculas de proteína. En el primer sistema las dos proteínas están inmersas únicamente en agua (representada como solvente explícito) y en el segundo sistema, además del solvente, se agregaron iones para investigar la influencia de cargas en la posible agregación de tau. A partir de una trayectoria de 1&#956;s a temperatura de 310 K, se analizaron los cambios estructurales que experimentaron los monómeros de tau. En ambos sistemas, las proteínas presentaron cambios importantes respecto a la configuración inicial; existiendo algunas diferencias en la estructura secundaria acorde a la presencia o ausencia de iones. Identificamos que, en ambos sistemas, no hay evidencia de un proceso agregativo. Los resultados aquí presentados corroboran que SIRAH no induce la formación de estructura secundaria espuria; la estructura secundaria obtenida es similar a la reportada con campos de fuerza atomísticos y, además, los resultados son similares a las observaciones con proteínas tau in vitro, validando así el empleo del campo de fuerza SIRAH para estudiar proteínas de gran tamaño, así como la factibilidad de alcanzar escalas temporales y espaciales cercanas a las experimentales. El análisis conformacional de las trayectorias obtenidas ofrece, por primera vez, una perspectiva desde la dinámica molecular del mecanismo de interacción de dos proteínas tau completas, lo cual contribuye a la comprensión del fenómeno y a la identificación de las regiones de interacción proteína-proteína.]]></p></abstract>
<abstract abstract-type="short" xml:lang="en"><p><![CDATA[Abstract Currently about 48 million people worldwide live with Alzheimer&#8217;s disease, the most common form of dementia, and still without cure. This disease is partially due to abnormal post-translational modifications in tau protein, that in turn induce its abnormal polymerization, forming fibrils and neurofibrillary tangles. Tau does not show a well-defined structure, known as intrinsically disordered protein. Molecular dynamics is an effective method to study this type of protein. In this work, this methodology was used in combination with the SIRAH (Southamerican Initiative for a Rapid and Accurate Hamiltonian) force field was employed to model two different systems of tau, each with two protein molecules. In the first system, the two proteins are immersed only in water (represented as an explicit solvent), in the second system, in addition to the solvent, ions were added to investigate whether the presence of charges induces protein self-aggregation. The structural modifications of tau were evaluated from 1 &#956;s trajectory at 310 K. For each system, the proteins showed important modifications compared to the initial structure; differences in the secondary structure were found according to the presence or absence of ions. Nevertheless, in both systems, there is no evidence of tau aggregation. These data demonstrated that SIRAH does not induce artificial secondary structures in tau; the obtained secondary structure is comparable with that reported using atomistic force fields; likewise, the results are similar to the observations of tau proteins in vitro studies, therefore this study validated the use of the SIRAH force field to study large proteins and the capacity to reach temporal and spatial scales similar to the experimental studies. In addition, the conformational analysis of the obtained trajectories suggests, for the first time, a molecular dynamics perspective that contributes to the understanding and identification of protein-protein interaction regions.]]></p></abstract>
<kwd-group>
<kwd lng="es"><![CDATA[Enfermedad de Alzheimer]]></kwd>
<kwd lng="es"><![CDATA[tau]]></kwd>
<kwd lng="es"><![CDATA[proteína intrínsicamente desordenada]]></kwd>
<kwd lng="es"><![CDATA[modelado de grano grueso]]></kwd>
<kwd lng="es"><![CDATA[SIRAH]]></kwd>
<kwd lng="en"><![CDATA[Alzheimer disease]]></kwd>
<kwd lng="en"><![CDATA[intrinsic disorder protein]]></kwd>
<kwd lng="en"><![CDATA[coarse-grained modeling]]></kwd>
<kwd lng="en"><![CDATA[SIRAH]]></kwd>
</kwd-group>
</article-meta>
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