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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
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dos Santos, Marlus Alves [1] ; Teixeira, Francesco Brugnera [2] ; Teixeira Moreira, Heline Hellen [2] ; Rodrigues, Adele Aud [1] ; Machado, Fabricio Castro [1] ; Clemente, Tatiana Mordente [1] ; Brigido, Paula Cristina [1] ; Silva, Rebecca Tavares E. [1] ; Purcino, Cecilio [1] ; Barbosa Gomes, Rafael Goncalves [1] ; Bahia, Diana [3, 4] ; Mortara, Renato Arruda [4] ; Munte, Claudia Elisabeth [2] ; Horjales, Eduardo [2] ; da Silva, Claudio Vieira [1]
Total Authors: 15
Affiliation:
[1] Univ Fed Uberlandia, Inst Ciencias Biomed, BR-38400 Uberlandia, MG - Brazil
[2] Univ Sao Paulo, Inst Fis Sao Carlos, Sao Carlos, SP - Brazil
[3] Univ Fed Minas Gerais, Inst Ciencias Biol, Dept Biol Geral, Belo Horizonte, MG - Brazil
[4] Univ Fed Sao Paulo, Escola Paulista Med, Dept Microbiol Imunol & Parasitol, Vila Mariana, SP - Brazil
Total Affiliations: 4
Document type: Journal article
Source: SCIENTIFIC REPORTS; v. 4, MAR 4 2014.
Web of Science Citations: 4
Abstract

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. (AU)

FAPESP's process: 10/51867-6 - SMOLBNET 2.0: Structural studies on proteins related to trypanosomatids infection and to complexes of these proteins with molecules which are involved in the infection process
Grantee:Eduardo Horjales Reboredo
Support type: Regular Research Grants
FAPESP's process: 12/21153-7 - Structural studies on Trypanosoma cruzi P21 protein as a strategy for Chagas Disease treatment
Grantee:Francesco Brugnera Teixeira
Support type: Scholarships in Brazil - Doctorate (Direct)