Deus, um Delírio by Richard Dawkins

By Richard Dawkins

Num pace de guerras e ataques terroristas com motivações religiosas, o movimento pró-ateísmo ganha força no mundo todo. E seu líder é o respeitado biólogo Richard Dawkins, eleito recentemente um dos três intelectuais mais importantes do mundo (junto com Umberto Eco e Noam Chomsky) pela revista inglesa Prospect. Autor de vários clássicos nas áreas de ciência e filosofia, ele sempre atestou a irracionalidade de acreditar em Deus e os terríveis danos que a crença já causou à sociedade. Agora, neste "Deus, um Delírio", seu intelecto afiado se concentra exclusivamente no assunto e mostra como a religião alimenta a guerra, fomenta o fanatismo e doutrina as crianças. O objetivo relevant deste texto mordaz é provocar: provocar os religiosos convictos, mas principalmente provocar os que são religiosos "por inércia", levando-os a pensar racionalmente e trocar sua "crença" pelo "orgulho ateu" e pela ciência. Dawkins despreza a idéia de que a religião mereça respeito especial, mesmo se moderada, e compara a educação religiosa de crianças ao abuso infantil. Para ele, falar de "criança católica" ou "criança muçulmana" é como falar de "criança neoliberal" - não faz sentido. O biólogo united states seu conceito de memes (idéias que agem como os genes) e o darwinismo para propor explicações à tendência da humanidade de acreditar num ser stronger. E desmonta um a um, com base na teoria das probabilidades, os argumentos que defendem a existência de Deus (ou Alá, ou qualquer tipo de ente sobrenatural), dedicando especial atenção ao "design inteligente", tentativa criacionista de harmonizar ciência e religião.

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I I I . Comparison of the primary structures of the large and small subunits obtained f r o m five species of Nicotiana. Biochim. biophys. Acta 236 (1971) 578-586. K A W A S H I M A , N. G. Studies on Fraction I protein. IV. Mode of inheritance of primary structure in relation to whether chlorophyll or nuclear D N A contains the code for a chloroplast protein. Biochim. biophys. Acta 2 6 2 ( 1 9 7 2 ) 42-49. C. and M A T H E S O N , A. A simplified purification and some properties of ribulose 1,5-diphosphate carboxylase f r o m barley.

By all the methods tried. Fraction I protein is inseparable by incubating w i t h M g from RBP carboxylase, and meets the criteria for homogeneity. /mg. 0 and 3 0 ° C . Contaminating proteins of high 3 specific activity are thus easy to overlook, and may account for the oxygenase a c t i v i t y . T w o observations are consistent w i t h this; firstly, the ratio of oxygenase t o carboxylase activity increases two-fold during purification of the oxygenase, and secondly, the carboxylase loses two-thirds of its 3 activity during three weeks storage While the oxygenase activity remains constant .

0 and 3 0 ° C . Contaminating proteins of high 3 specific activity are thus easy to overlook, and may account for the oxygenase a c t i v i t y . T w o observations are consistent w i t h this; firstly, the ratio of oxygenase t o carboxylase activity increases two-fold during purification of the oxygenase, and secondly, the carboxylase loses two-thirds of its 3 activity during three weeks storage While the oxygenase activity remains constant . These observations do not prove that the oxygenase is a contaminant, since selective denaturation of distinct active sites may account for them, but it is clear that more evidence is needed t o confirm that the oxygenase activity is a property of Fraction I protein.

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