4 research outputs found
The Johannine Community as a Constructed, Imagined Community
The article takes issue with recent attempts to deny that the New Testament Gospels were addressed to distinct early Christian communities and argues that it is still meaningful to trace how these writings construct distinct early Christian identities. The author applies the social identity approach and concepts related to the symbolic construction of communities and imagined communities to explain how an ideal portrait of the community of Jesus’ followers is created in the Gospel of John. The article argues that this portrait constructs social reality rather than reflects it in any transparent way. The author demonstrates how John anchors his story of Jesus to mythical beginnings and uses various dualistic polarities to express a clear demarcation between Jesus’ followers and the rest of world. In the Gospel, the knowledge of God communicated only by Jesus and the mutual love between Jesus’ disciples function as strong symbols of belonging for Jesus’ followers but also create an imagined boundary between them and those who have not received Jesus’ revelation. The author argues that the Gospel writer has embedded his story of Jesus in a mythical framework in order to naturalize and essentialize a distinct early Christian social identity that was actually blurred and in the making.Peer reviewe
Domino Reactions of Amidines with Methyl 2-Chloro-2-cyclopropylideneacetate as an Efficient Access to Cyclobutene-Annelated Pyrimidinones †
DNA bending and a flip-out mechanism for base excision by the helix–hairpin–helix DNA glycosylase, Escherichia coli AlkA
The Escherichia coli AlkA protein is a base excision repair glycosylase that removes a variety of alkylated bases from DNA. The 2.5 Å crystal structure of AlkA complexed to DNA shows a large distortion in the bound DNA. The enzyme flips a 1–azaribose abasic nucleotide out of DNA and induces a 66° bend in the DNA with a marked widening of the minor groove. The position of the 1–azaribose in the enzyme active site suggests an S(N)1-type mechanism for the glycosylase reaction, in which the essential catalytic Asp238 provides direct assistance for base removal. Catalytic selectivity might result from the enhanced stacking of positively charged, alkylated bases against the aromatic side chain of Trp272 in conjunction with the relative ease of cleaving the weakened glycosylic bond of these modified nucleotides. The structure of the AlkA–DNA complex offers the first glimpse of a helix–hairpin–helix (HhH) glycosylase complexed to DNA. Modeling studies suggest that other HhH glycosylases can bind to DNA in a similar manner
