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Structures of a bi-functional Kunitz-type STI family inhibitor of serine and aspartic proteases: Could the aspartic protease inhibition have evolved from a canonical serine protease-binding loop?
ArticleAbstract: Bi-functional inhibitors from the Kunitz-type soybean trypsin inhibitor (STI) family are glycosylatePalabras claves:Aspartic protease inhibitors, Bi-functional inhibitors, Kunitz-type STI family inhibitors, Plant protease inhibitors, β-Trefoil foldAutores:Berry C., Pons T., Rudino-Pinera E., Valiente P.A., Yasel GuerraFuentes:googlescopusThe Stability Landscape of de novo TIM Barrels Explored by a Modular Design Approach
ArticleAbstract: The ability to design stable proteins with custom-made functions is a major goal in biochemistry witPalabras claves:(β/α) -barrel 8, de novo protein design, non-additive effects, protein folding and stability, stability landscapeAutores:Baker D., Costas M., Fernández-Velasco D.A., Höcker B., Kordes S., Rodríguez-Romero A., Rojas-Ortega E., Romero-Romero S., Shanmugaratnam S., Silva Manzano D.A., Tapia C., Yasel GuerraFuentes:googlescopus