Neste artigo é abordada a sentença nietzschiana "Deus está morto" trazida principalmente no aforismo 145 de "A gaia ciência" e como esse pensamento serviu de base para construção de uma forma de superar o homem que surgiu após essa secularização anunciada por Nietzsche. O pós-humano evidencia a superação do homem da verdade científica, trazendo uma nova ontologia para o mundo da tecnologia, com uma simbiose entre o corpo biológico do "homem-deus" e da máquina computacional tecnológica.
This work was supported by Fundacao para a Ciencia e a Tecnologia - Ministerio da Ciencia, Tecnologia e Ensino Superior (FCT-MCTES, Portugal) projects PTDC/QUI-BIQ/112929/2009, PTDC/SAU-ENB/117013/2010 and PTDC/BBB-BQB/3494/2014, Calouste Gulbenkian Foundation (FCG, Portugal) project Science Frontiers Research Prize 2010, European Union Marie Sklodowska-Curie Research and Innovation Staff Exchange H2020-MSCA-RISE-2014 project INPACT (Grant 644167), Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq, Brazil, grant numbers 471239/2012-7 and 306669/2013-7) and Fundacao Carlos Chagas Filho de Amparo a Pesquisa do Estado do Rio de Janeiro (FAPERJ, Brazil, grant numbers E-26/110.636/2012, E-26/110.092/2013 and E-26/201.167/2014). AFF acknowledges FCT-MCTES fellowship SFRH/BD/77609/2011. MS acknowledges FCT-MCTES fellowship PD/BD/128202/2016. ICM acknowledges consecutive funding from the FCT-MCTES fellowship SFRH/BPD/74287/2010 and the Program "Investigador FCT" (IF/00772/2013 Research Contract). This work was also supported by LISBOA01-0145-FEDER-007391 project, cofunded by FEDER, through POR Lisboa 2020 -Programa Operacional Regional de Lisboa, PORTUGAL 2020, and Fundacao para a Ciencia e a Tecnologia. The NMR spectrometers at FCT NOVA are part of Rede Nacional de RMN (PTNMR), supported by FCT-MCTES (ROTEIRO/0031/2013 - PINFRA/22161/2016) co-funded by FEDER through COMPETE 2020, POCI, and PORL and FCT through PIDDAC. ; Understanding protein structure and dynamics, which govern key cellular processes, is crucial for basic and applied research. Intrinsically disordered protein (IDP) regions display multifunctionality via alternative transient conformations, being key players in disease mechanisms. IDP regions are abundant, namely in small viruses, allowing a large number of functions out of a small proteome. The relation between protein function and structure is thus now seen from a different perspective: as IDP regions enable transient structural arrangements, each conformer can play different roles within the cell. However, as IDP regions are hard and time-consuming to study via classical techniques (optimized for globular proteins with unique conformations), new methods are required. Here, employing the dengue virus (DENV) capsid (C) protein and the immunoglobulin-binding domain of streptococcal protein G, we describe a straightforward NMR method to differentiate the solvent accessibility of single amino acid N-H groups in structured and IDP regions. We also gain insights into DENV C flexible fold region biological activity. The method, based on minimal pH changes, uses the well-established 1 H- 15 N HSQC pulse sequence and is easily implementable in current protein NMR routines. The data generated are simple to interpret, with this rapid approach being an useful first-choice IDPs characterization method. ; publishersversion ; published
