<?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>0187-893X</journal-id>
<journal-title><![CDATA[Educación química]]></journal-title>
<abbrev-journal-title><![CDATA[Educ. quím]]></abbrev-journal-title>
<issn>0187-893X</issn>
<publisher>
<publisher-name><![CDATA[Universidad Nacional Autónoma de México, Facultad de Química]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S0187-893X2025000100005</article-id>
<article-id pub-id-type="doi">10.22201/fq.18708404e.2025.1.89902</article-id>
<title-group>
<article-title xml:lang="es"><![CDATA[Desentrañando los secretos de autoensamblado en las máquinas de la vida: plegamiento de proteínas y Nobel de Química 2024]]></article-title>
<article-title xml:lang="en"><![CDATA[Unraveling the Secrets of Self-Assembly in the Machines of Life: Protein Folding and the 2024 Nobel Prize in Chemistry]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Rodriguez-Sotres]]></surname>
<given-names><![CDATA[Rogelio]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Aguayo-Ortíz]]></surname>
<given-names><![CDATA[Rodrigo]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Universidad Nacional Autónoma de México Facultad de Química ]]></institution>
<addr-line><![CDATA[ ]]></addr-line>
<country>México</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>00</month>
<year>2025</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>00</month>
<year>2025</year>
</pub-date>
<volume>36</volume>
<numero>1</numero>
<fpage>5</fpage>
<lpage>13</lpage>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_arttext&amp;pid=S0187-893X2025000100005&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_abstract&amp;pid=S0187-893X2025000100005&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_pdf&amp;pid=S0187-893X2025000100005&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="es"><p><![CDATA[Resumen En 2024, el premio Nobel de Química fue concedido a Demis Hassabis, John M. Jumper y David Baker por sus aportes a la predicción computacional del plegamiento y al diseño de proteínas. Sus desarrollos han contribuido a estudiar de modo más rápido y eficaz la función de estas moléculas biológicas que hacen el trabajo duro en los seres vivos. Formadas por 20 diferentes aminoácidos combinados en secuencias variables, cada proteína se pliega de una o más formas, según su secuencia, lo que determina su función en la célula. Aunque la secuencia de los aminoácidos codifica la forma final, el código no ha sido descifrado del todo y determinar la forma requiere de técnicas experimentales, laboriosas, caras y falibles. La genómica ha revelado más de 200 millones de secuencias naturales de aminoácidos, pero la Biología estructural ha resuelto apenas unas 220 mil estructuras. Hoy, la brecha se ha reducido, gracias al desarrollo de poderosas herramientas de Inteligencia Artificial (IA) por parte de los investigadores galardonados. Estos nuevos desarrollos han traído beneficios en el avance de la Medicina, la Farmacología, la Biotecnología y otras disciplinas. En México y el resto de Latinoamérica hay investigadores activos en el campo y el futuro es promisorio.]]></p></abstract>
<abstract abstract-type="short" xml:lang="en"><p><![CDATA[Abstract In 2024, the Nobel Prize in Chemistry was awarded to Demis Hassabis, John M. Jumper, and David Baker for their contributions to computational protein folding prediction and design. Their advancements have enabled faster and more efficient study of the functions of these biological molecules, which perform the heavy lifting in living organisms. Composed of 20 different amino acids arranged in variable sequences, each protein folds into one or more structures based on its sequence, which determines its cellular function. Although the amino acid sequence encodes the final shape, the code has not been fully deciphered, and determining the structure requires experimental techniques that are labor-intensive, expensive, and not infallible. Genomics has revealed over 200 million natural amino acid sequences, yet Structural Biology has resolved only about 220,000 structures. Today, the gap has narrowed, thanks to the development of powerful Artificial Intelligence (AI) tools by the laureates. These breakthroughs have brought benefits to the advancement of Medicine, Pharmacology, Biotechnology, and other fields. In Mexico and the rest of Latin America, there are active researchers in the field, and the future looks promising.]]></p></abstract>
<kwd-group>
<kwd lng="es"><![CDATA[Premio Nobel]]></kwd>
<kwd lng="es"><![CDATA[bioquímica]]></kwd>
<kwd lng="es"><![CDATA[interdisciplinaridad]]></kwd>
<kwd lng="es"><![CDATA[plegamiento de proteínas]]></kwd>
<kwd lng="es"><![CDATA[inteligencia artificial]]></kwd>
<kwd lng="es"><![CDATA[proteínas artificiales]]></kwd>
<kwd lng="es"><![CDATA[química computacional]]></kwd>
<kwd lng="en"><![CDATA[Nobel Prize]]></kwd>
<kwd lng="en"><![CDATA[biochemistry]]></kwd>
<kwd lng="en"><![CDATA[interdisciplinarity]]></kwd>
<kwd lng="en"><![CDATA[protein folding]]></kwd>
<kwd lng="en"><![CDATA[artificial intelligence]]></kwd>
<kwd lng="en"><![CDATA[artificial proteins]]></kwd>
<kwd lng="en"><![CDATA[computational chemistry]]></kwd>
</kwd-group>
</article-meta>
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