{"id":131460,"date":"1996-01-01T00:00:00","date_gmt":"1996-01-01T00:00:00","guid":{"rendered":"https:\/\/www.deberes.net\/tesis\/sin-categoria\/estructura-de-la-catalasa-hpii-de-escherichia-coli\/"},"modified":"1996-01-01T00:00:00","modified_gmt":"1996-01-01T00:00:00","slug":"estructura-de-la-catalasa-hpii-de-escherichia-coli","status":"publish","type":"post","link":"https:\/\/www.deberes.net\/tesis\/quimica\/estructura-de-la-catalasa-hpii-de-escherichia-coli\/","title":{"rendered":"Estructura de la catalasa hpii de escherichia coli."},"content":{"rendered":"<h2>Tesis doctoral de <strong> Jer\u00f3nimo Bravo  Sicilia <\/strong><\/h2>\n<p>En el presente estudio se ha abordado la determinacion estructural, mediante cristalografia de proteinas de la catalasa hpii de escherichia coli.Se ha determinado la estructura tridimensional de la catalasa nativa a 1.9 a de resolucion. Asimismo se han determinado las estructuras de las catalasas hpii recombinantes n201h y n201a a 2.2a de resolucion; h12n a 2.1a y h128n a 1.9a de resolucion. Tambien se ha determinado la estructura del complejo de catalasa hpii con azida a 2.2a.  el analisis de todas estas estructuras ha puesto de manifiesto que la catalasa de hpii es un tetramero organizado de acuerdo con la simetria del grupo puntual 222, que la region central de la molecual presenta una elevada homolog\u00eda estructural con otras estructuras de catalasas. Los residuos del brazo aminoterminal y undominio carboxiterminal extra suponen las mayores diferencias (unos 350 residuos) entre las estructuras de hpii y catalasa de higado bovino que es la que se utilizo en la resolucion de hpii por reemplazo molecular. Se ha caracterizado un nuevo grupo hemo en la hpii nativa y los mutantes activos.<\/p>\n<p>&nbsp;<\/p>\n<h3>Datos acad\u00e9micos de la tesis doctoral \u00ab<strong>Estructura de la catalasa hpii de escherichia coli.<\/strong>\u00ab<\/h3>\n<ul>\n<li><strong>T\u00edtulo de la tesis:<\/strong>\u00a0 Estructura de la catalasa hpii de escherichia coli. <\/li>\n<li><strong>Autor:<\/strong>\u00a0 Jer\u00f3nimo Bravo  Sicilia <\/li>\n<li><strong>Universidad:<\/strong>\u00a0 Polit\u00e9cnica de catalunya<\/li>\n<li><strong>Fecha de lectura de la tesis:<\/strong>\u00a0 01\/01\/1996<\/li>\n<\/ul>\n<p>&nbsp;<\/p>\n<h3>Direcci\u00f3n y tribunal<\/h3>\n<ul>\n<li><strong>Director de la tesis<\/strong>\n<ul>\n<li>Ignacio Fita Rodriguez<\/li>\n<\/ul>\n<\/li>\n<li><strong>Tribunal<\/strong>\n<ul>\n<li>Presidente del tribunal: Juan  Antonio Subirana Torrent <\/li>\n<li>Lucy Malinina (vocal)<\/li>\n<li>Peter Loewen (vocal)<\/li>\n<li>Francesc Xavier Avil\u00e9s Puigvert (vocal)<\/li>\n<\/ul>\n<\/li>\n<\/ul>\n<p>&nbsp;<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Tesis doctoral de Jer\u00f3nimo Bravo Sicilia En el presente estudio se ha abordado la determinacion estructural, mediante cristalografia de proteinas [&hellip;]<\/p>\n","protected":false},"author":1,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"site-sidebar-layout":"default","site-content-layout":"","ast-site-content-layout":"","site-content-style":"default","site-sidebar-style":"default","ast-global-header-display":"","ast-banner-title-visibility":"","ast-main-header-display":"","ast-hfb-above-header-display":"","ast-hfb-below-header-display":"","ast-hfb-mobile-header-display":"","site-post-title":"","ast-breadcrumbs-content":"","ast-featured-img":"","footer-sml-layout":"","theme-transparent-header-meta":"","adv-header-id-meta":"","stick-header-meta":"","header-above-stick-meta":"","header-main-stick-meta":"","header-below-stick-meta":"","astra-migrate-meta-layouts":"default","ast-page-background-enabled":"default","ast-page-background-meta":{"desktop":{"background-color":"var(--ast-global-color-4)","background-image":"","background-repeat":"repeat","background-position":"center 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