LEA_4 motifs function alone and in conjunction with synergistic cosolutes to protect a labile enzyme during desiccation.

Organisms from all kingdoms of life depend on Late Embryogenesis Abundant (LEA) proteins to survive desiccation. LEA proteins are divided into broad families distinguished by the presence of family-specific motif sequences. The LEA_4 family, characterized by 11-residue motifs, plays a crucial role in the desiccation tolerance of numerous species.

Disordered proteins interact with the chemical environment to tune their protective function during drying.

The conformational ensemble and function of intrinsically disordered proteins (IDPs) are sensitive to their solution environment. The inherent malleability of disordered proteins, combined with the exposure of their residues, accounts for this sensitivity. One context in which IDPs play important roles that are concomitant with massive changes to the intracellular environment is during desiccation (extreme drying).

Protein surface chemistry encodes an adaptive tolerance to desiccation.

Cellular desiccation - the loss of nearly all water from the cell - is a recurring stress in an increasing number of ecosystems that can drive protein unfolding and aggregation. For cells to survive, at least some of the proteome must resume function upon rehydration. Which proteins tolerate desiccation, and the molecular determinants that underlie this tolerance, are largely unknown.

Transformative Insights: Break Up with Salt (BUWS) Program's Short-Term Influence on Hypertension Risk Factors.

Break Up with Salt (BUWS) is a four-session community-based nutrition education program aimed at reducing key controllable hypertension risk factors. This pilot study utilized a pre-post survey design to assess short-term outcomes on food behaviors (including DASH diet eating patterns), physical activity, and overall well-being, in two groups of participants. The first "pilot" group (n = 25) completed a comprehensive, 16-item survey; the second "abbreviated" group (n = 27) completed a 5-item survey.

Labile assembly of a tardigrade protein induces biostasis.

Tardigrades are microscopic animals that survive desiccation by inducing biostasis. To survive drying tardigrades rely on intrinsically disordered CAHS proteins, which also function to prevent perturbations induced by drying in vitro and in heterologous systems. CAHS proteins have been shown to form gels both in vitro and in vivo, which has been speculated to be linked to their protective capacity.