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Molecular Mechanism for LAMP1 Recognition by Lassa Virus.

Lassa VIRUS LAMP-1 receptor-recognition-arenaviruses internalizing 3Dciencia

Cannabinoid Receptor

cb1 rc cannabinoid receptor am6538 antagonist anandamide thc seven transmembrane helix 7TMH Rc

Human Nuclear pore complex

Nuclear pore complex

Myoglobin molecule structure Chocolate

myoglobin molecule kendrew-mioglobina-chocolate bombon hemo white

Artemisinin or qinghaosu, antimalarial drug.

Artemisinin, also called qinghaosu, antimalarial drug derived from the sweet wormwood plant, Artemisia annua. Artemisinin is a sesquiterpene lactone (a compound made up of three isoprene units bound to cyclic organic esters) and is distilled from the dried leaves or flower clusters of A. annua.

Chemistry Nobel for mechanistic studies of DNA Repair

Centro activo de la enzima reparadora de errores AlkB (azul y naranja) en el genoma en este caso 1 metil-adenina. Una de las hebras del ADN de doble cadena (amarillo) presenta una adenina metilada (1-meA) un daño común de los genoma. Esta adenina y el grupo metilo (rosa) se muestra como modelo de bolas y palos. El átomo de Hierro II (verde) en este caso está relacionado con la catalisis E. coli AlkB protein is a direct dealkylation DNA repair protein. It perform the oxidative demethylation of DNA base lesions 1-meA, 3-meC, 1-meG and 3-meT. AlkB also removes etheno DNA lesions, by using a similar oxidation mechanism. Human homolog ABH2 has the same role of guarding mammalian genomes against 1-meA damage by repairing this lesion in double-stranded DNA (dsDNA).

La enzima prodigiosa de verdad, la anhidrasa.

There are three distinct classes of CAs (designated α, β and γ) that have no significant sequence identity and were invented independently. Thus, the carbonic anhydrase classes are excellent examples of convergent evolution of catalytic function.

Icosahedral Virus Families

virus icosahedric families evolution familias capsides icosaedricas structure evolucion infografia infographics blue tongue BTV picorna like PRD1 HK97 reoviridae adenovirus

HK96 virus Escher schwan fold

The HK97 capsid is formed by the arrangement of 420 protein chains into 60 hexamers (Orange-white) and 12 pentamers (Red). The HK97 fold is present not only in a large number of dsDNA bacteriophage capsids, including the T-phages, lambdoid phages, etc, but also in the major capsid protein of eukaryotic herpesviruses. it seems like an escher icosahedron.

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