<?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>S0187-893X2018000300003</article-id>
<article-id pub-id-type="doi">10.22201/fq.18708404e.2018.3.64699</article-id>
<title-group>
<article-title xml:lang="es"><![CDATA[Estabilidad termodinámica de proteínas]]></article-title>
<article-title xml:lang="en"><![CDATA[Protein Thermodynamic Stability]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Romero-Romero]]></surname>
<given-names><![CDATA[Sergio]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Fernández-Velasco]]></surname>
<given-names><![CDATA[D. Alejandro]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Costas]]></surname>
<given-names><![CDATA[Miguel]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,Universidad Nacional Autónoma de México Facultad de Medicina Departamento de Bioquímica]]></institution>
<addr-line><![CDATA[México ]]></addr-line>
<country>Mexico</country>
</aff>
<aff id="Af2">
<institution><![CDATA[,Universidad Nacional Autónoma de México Facultad de Química Departamento de Fisicoquímica]]></institution>
<addr-line><![CDATA[México ]]></addr-line>
<country>Mexico</country>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>00</month>
<year>2018</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>00</month>
<year>2018</year>
</pub-date>
<volume>29</volume>
<numero>3</numero>
<fpage>3</fpage>
<lpage>17</lpage>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_arttext&amp;pid=S0187-893X2018000300003&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_abstract&amp;pid=S0187-893X2018000300003&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.mx/scielo.php?script=sci_pdf&amp;pid=S0187-893X2018000300003&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="es"><p><![CDATA[Resumen Las proteínas llevan a cabo una gran variedad de funciones debido a la estructura que adoptan en el estado nativo. El estado nativo está en equilibrio con un gran número de conformaciones inactivas que colectivamente son llamadas estado desnaturalizado. A partir de experimentos de calorimetría diferencial de barrido (CDB), es posible obtener la estabilidad termodinámica de la proteína, esto es el cambio de energía libre de Gibbs (&#916;G) entre el estado nativo y el desnaturalizado, así como determinar la curva de estabilidad (variación del &#916;G con la temperatura). En este trabajo describimos los principios generales de la CDB, discutimos de qué manera es posible determinar la curva estabilidad, y proporcionamos ejemplos de las curvas de estabilidad obtenidas para diferentes proteínas con topología de barril TIM.]]></p></abstract>
<abstract abstract-type="short" xml:lang="en"><p><![CDATA[Abstract Proteins are able to perform a great variety of functions when they are in their native state. This state is in equilibrium with a large number of inactive conformations that collectively are called the denatured state. Using differential scanning calorimetry (DSC), it is possible to evaluate the protein thermodynamic stability, i.e. the change in Gibbs free energy (&#916;G) between the native and the denatured state, as well as the stability curve (variation of &#916;G with temperature). In this work, we describe the general principles of DSC, discuss how to obtain the stability curve, and provide examples of stability curves for different proteins with TIM barrel topology.]]></p></abstract>
<kwd-group>
<kwd lng="es"><![CDATA[Termodinámica]]></kwd>
<kwd lng="es"><![CDATA[Proteínas]]></kwd>
<kwd lng="es"><![CDATA[Estabilidad]]></kwd>
<kwd lng="es"><![CDATA[Calorimetría]]></kwd>
<kwd lng="es"><![CDATA[Barril TIM]]></kwd>
<kwd lng="en"><![CDATA[Thermodynamic]]></kwd>
<kwd lng="en"><![CDATA[Proteins]]></kwd>
<kwd lng="en"><![CDATA[Stability]]></kwd>
<kwd lng="en"><![CDATA[Calorimetry]]></kwd>
<kwd lng="en"><![CDATA[TIM barrel]]></kwd>
</kwd-group>
</article-meta>
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