A successful strategy for the recovering of active P21, an insoluble recombinant protein of Trypanosoma cruzi

• Autor(a) principal: Santos, Marlus Alves dos
• Data de Publicação: 2014
• Outros Autores: Teixeira, Francesco Brugnera, Teixeira Moreira, Heline Hellen, Rodrigues, Adele Aud, Machado, Fabricio Castro, Clemente, Tatiana Mordente, Brigido, Paula Cristina, Silva, Rebecca Tavares E., Purcino, Cecilio, Barbosa Gomes, Rafael Goncalves, Bahia, Diana [UNIFESP], Mortara, Renato Arruda [UNIFESP], Munte, Claudia Elisabeth, Horjales, Eduardo, Silva, Claudio Vieira da
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UNIFESP
• Texto Completo: http://repositorio.unifesp.br/handle/11600/37539; http://dx.doi.org/10.1038/srep04259

Structural studies of proteins normally require large quantities of pure material that can only be obtained through heterologous expression systems and recombinant technique. in these procedures, large amounts of expressed protein are often found in the insoluble fraction, making protein purification from the soluble fraction inefficient, laborious, and costly. Usually, protein refolding is avoided due to a lack of experimental assays that can validate correct folding and that can compare the conformational population to that of the soluble fraction. Herein, we propose a validation method using simple and rapid 1D H-1 nuclear magnetic resonance (NMR) spectra that can efficiently compare protein samples, including individual information of the environment of each proton in the structure.