Re/turning to soil: becoming one-bodied with the Earth.

This paper curates four experiential narratives and poetry by the five co-authors that illustrate epistemic and ontic shift from the Modern Western (ModWest) mindset to a holistic, embodied and animistic mindset. Coming from different cultural backgrounds, yet having been systemically influenced by the dominant ModWest views and values, each author has initiated an ongoing shift in consciousness, demonstrating how such transformations are possible. Affirming that a shift in consciousness is not simply a matter of cognitive change but is a thoroughly holistic process, the authors write in autobiographical narratives and poetry to capture and convey embodied and emplaced, experiential understanding and feelings, or 'felt sense.' Deep changes in the consciousness, such as these epistemic shifts, take the whole ensemble of "body + mind + heart + soul + spirit + the world" as the unit of change for learning. Through these writings, they sensuously and feelingly, existentially-and-spiritually and discursively explore possibilities of becoming one-bodied with the animate Earth. They call this the re-bonding project through which they address humanity's first-order bonding rupture between Humans and the Earth community.

Direct observations of shifts in the ß-sheet register of a protein-peptide complex using explicit solvent simulations.

Using explicit solvent molecular dynamics simulations, we were able to obtain direct observations of shifts in the hydrogen-bonding register of an intermolecular ß-sheet protein-peptide complex. The ß-sheet is formed between the FHA domain of cancer marker protein Ki67 (Ki67FHA) and a peptide fragment of the hNIFK signaling protein. Potential encounter complexes of the Ki67FHA receptor and hNIFK peptide are misregistered states of the ß-sheet. Rearrangements of one of these misregistered states to the native state were captured in three independent simulations. All three rearrangements occurred by a common mechanism: an aromatic residue of the peptide (F263) anchors into a transient hydrophobic pocket of the receptor to facilitate the formation of native hydrogen bonds. To our knowledge, these simulations provide the first atomically detailed visualizations of a mechanism by which nature might correct for errors in the alignment of intermolecular ß-sheets.