Predestination and freedom in Milton's 'Paradise lost'

John Milton's epic poem Paradise Lost (1667) offers a highly creative seventeenth-century reconstruction of the doctrine of predestination, a reconstruction which both anticipates modern theological developments and sheds important light on the history of predestinarian thought. Moving beyond the framework of post-Reformation controversies, the poem emphasises both the freedom and the universality of electing grace, and the eternally decisive role of human freedom in salvation. The poem erases the distinction between an eternal election of some human beings and an eternal rejection of others, portraying reprobation instead as the temporal self-condemnation of those who wilfully reject their own election and so exclude themselves from salvation. While election is grounded in the gracious will of God, reprobation is thus grounded in the fluid sphere of human decision. Highlighting this sphere of human decision, the poem depicts the freedom of human beings to actualise the future as itself the object of divine predestination. While presenting its own unique vision of predestination, Paradise Lost thus moves towards the influential and distinctively modern formulations of later thinkers like Schleiermacher and Barth.

MiAMP1, a novel protein from Macadamia integrifolia adopts a Greek key beta-barrel fold unique amongst plant antimicrobial proteins

MiAMP1 is a recently discovered 76 amino acid residue, highly basic protein from the nut kernel of:Macadamia integrifolia which possesses no sequence homology to any known protein and inhibits the growth of several microbial plant pathogens in vitro while having no effect on mammalian or plant cells. It is considered to be a potentially useful tool for the genetic engineering of disease resistance in transgenic crop plants and for the design of new fungicides. The three-dimensional structure of MiAMP1 was determined through homonuclear and heteronuclear (N-15) 2D NMR spectroscopy and subsequent simulated annealing calculations with the ultimate aim of understanding the structure-activity relationships of the protein. MiAMP1 is made up of eight beta-strands which are arranged in two Greek key motifs. These Greek key motifs associate to form a Greek key beta-barrel. This structure is unique amongst plant antimicrobial proteins and forms a new class which we term the beta-barrelins. Interestingly, the structure of MiAMP1 bears remarkable similarity to a yeast killer toxin from Williopsis mrakii. This toxin acts by inhibiting beta-glucan synthesis and thereby cell wall construction in sensitive strains of yeast. The structural similarity of MiAMP1 and WmKT, which originate from plant and fungal phyla respectively, may reflect a similar mode of action. (C) 1999 Academic Press.