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"From Edith Stein's comment that "being is the unfolding of meaning," the author contends that her understanding of the term is relational and thus resistant to both existentialism and essentialism. He tests his hypothesis against Stein's three modes of being (actual, essential, and mental) from both phenomenological and scholastic perspectives"--
The word revolution has a number of definitions (The American Heritage Dictionary, 2006). The one most pertinent to this series and volume is 'a sudden or momentous change in a situation'. Recent years have seen an unprecedented explosion of interest in unfolded proteins in all of their various forms. Coupled with this increase in interest we have seen momentous changes in the way unfolded proteins are viewed. Two particular paradigms have come under close scrutiny: unfolded proteins are disordered random coils devoid of persistent structure, and protein function first requires protein structure. The first of these is currently a hotly debated subject. The second paradigm we can safely claim has been overturned. There is a second definition of revolution that is quite relevant to a significant portion of the work reviewed herein, in particular those chapters dealing with local and persistent structure in unfolded proteins. That definition is 'a turning or rotational motion about an axis' (The American Heritage Dictionary, 2006). About four decades ago, Charles Tanford (1968) demonstrated that highly denatured proteins possess hydrodynamic properties consistent with Paul Flory's random coil (Flory, 1969). Given that the Flory random coil definition included the stipulation that conformers making up the denatured state ensemble would differ in energy by just a few kT, there has been the assumption that denatured states must therefore be completely random in nature with no persistent structure or biases towards particular conformers. Notably however, Tanford did note the random coil-like hydrodynamic data he obtained did not necessarily rule out the presence of structure in denatured proteins (Tanford, 1968). Around the same time, Sam Krimm and M. Lois Tiffany noted that the CD spectra they obtained for proteins in the presence of high concentration of chemical denaturants had similarities to spectra obtained for homopolymers of proline, lysine, and glutamic acid in water (Tiffany and Krimm, 1968a, 1968b, 1973, 1974). Homopolymers of these residues were known to adopt the left-handed polyproline II conformation, leading Tiffany and Krimm to hypothesise that highly denatured proteins possess significant polyproline II helix content. Of these two views, that espousing the lack of structure in denatured proteins became more widely adopted and was, over time, adopted as a central paradigm in protein folding. As several of the chapters in this volume note, a Tiffany and Krimm-like view appears to be, to some extent, the more correct one. The level to which it is correct is still unknown, although it is clear that the polyproline II helical conformation is not the only, perhaps not even the most common, persistent conformation present in unfolded proteins. Thus we have come through a full circle or revolution. (from the preface)
Truth's Triumph; or a Witness to the Two Witnesses from that unfolded parable of our Lord and Saviour Jesus Christ, ... Matthew. Chap. 13. verse 30 to 42 ... Written in the year ... 1676; transcribed by the author, with some alterations, 1690, etc by Thomas Tomkinson Pdf
Dreams of Archives Unfolded by Jocelyn Fenton Stitt Pdf
Introduction: Archival dreams and Caribbean life writing -- 'Autobiography in a graveyard' : doors of no return and revolutionary failures -- Speculative autobiography : ghosts and feminist fugitivity -- Repicturing the picturesque : genealogical desire, archives, and descendant community autobiography -- Ashes to ashes, dust to dust : Indo-Caribbean archival impossibility -- "Put my mom in there" : Memorialization as Caribbean counter-archive -- Coda: Untelling history.