Innovative recruitment strategies for a comprehensive worksite wellness initiative.

Recruiting for wellness initiatives is challenging. WorkWell KS, a statewide worksite wellness initiative, offers unique worksite recruitment strategies that may serve as lessons. From 2012 to 2018, WorkWell KS utilized champions, well-connected local leaders, to recruit worksites. A total of 784 worksites were recruited for at least one WorkWell KS workshop. A survey of champions requested identification of strategies, barriers and facilitators for successful recruitment and continued engagement. Forty-three champions reported on recruitment experiences. Sixty-three percent of respondents attributed recruitment success to having funding to complete their work. Face-to-face meetings was the most commonly reported successful strategy. Eighty-six percent of respondents reported that improving employee health was motivation for worksites to participate. Champions with a significant funding incentive for worksites commonly indicated that funding was a motivating factor. The most commonly selected factor for continued engagement was having a worksite staff member with wellness in their job description (67% of respondents). Forty-nine percent of respondents reported worksites' lack of time as a barrier to participation. The WorkWell KS initiative has implemented innovative recruitment methods that leverage well-connected leaders to recruit worksites to participate in a comprehensive worksite wellness initiative. Future worksite-based initiatives may benefit from adopting recruitment strategies presented here.

Biological Roles of Protein Kinetic Stability.

A protein's stability may range from nonexistent, as in the case of intrinsically disordered proteins, to very high, as indicated by a protein's resistance to degradation, even under relatively harsh conditions. The stability of this latter group is usually under kinetic control because of a high activation energy for unfolding that virtually traps the protein in a specific conformation, thereby conferring resistance to proteolytic degradation and misfolding aggregation. The usual outcome of kinetic stability is a longer protein half-life. Thus, the protective role of protein kinetic stability is often appreciated, but relatively little is known about the extent of biological roles related to this property. In this Perspective, we will discuss several known or putative biological roles of protein kinetic stability, including protection from stressors to avoid aggregation or premature degradation, achieving long-term phenotypic change, and regulating cellular processes by controlling the trigger and timing of molecular motion. The picture that emerges from this analysis is that protein kinetic stability is involved in a myriad of known and yet to be discovered biological functions via its ability to confer degradation resistance and control the timing, extent, and permanency of molecular motion.

Analyzing bean extracts using time-dependent SDS trapping to quantify the kinetic stability of phaseolin proteins.

In common beans and lima bean, the storage protein phaseolin is difficult to degrade and SDS-resistant, a sign of kinetic stability. Kinetically stable proteins (KSPs) are characterized by having a high-energy barrier between the native and denatured states that results in very slow unfolding. Such proteins are resistant to proteolytic degradation and detergents, such as SDS. Here the method SDS-Trapping of Proteins (S-TraP) is applied directly on bean extracts to quantify the kinetic stability of phaseolin in lima bean and several common beans, including black bean, navy bean, and small red bean. The bean extracts were incubated in SDS at various temperatures (60-75 °C) for different time periods, followed by SDS-PAGE analysis at room temperature, and subsequent band quantification to determine the kinetics of phaseolin unfolding. Eyring plot analysis showed that the phaseolin from each bean has high kinetic stability, with an SDS-trapping (i.e. unfolding) half-life ranging from about 20-100 years at 24 °C and 2-7 years at 37 °C. The remarkably high kinetic stability of these phaseolin proteins is consistent with the low digestibility of common beans and lima bean, as well as their relatively high germination temperatures. From a practical perspective, this work exemplifies that S-TraP is a useful and cost-effective method for quantifying the kinetic stability of proteins in biological extracts or lysates. Depending on the protein to be studied and its abundance, S-TraP may be performed directly on the extract without need for protein purification.

Perceptions versus interpretations, and domains for self-fulfilling prophesies.

I suggest two ways in which Jussim's extensive discussion (in his 2012 book) could be enriched: first, by exploring the distinction between perceptual judgments and interpretive judgments; second, by considering the power of expectations to be self-fulfilling in the case of young children and the case of fragile egos.

Kinetic Stability of Proteins in Beans and Peas: Implications for Protein Digestibility, Seed Germination, and Plant Adaptation.

Kinetically stable proteins (KSPs) are resistant to the denaturing detergent sodium dodecyl sulfate (SDS). Such resilience makes KSPs resistant to proteolytic degradation and may have arisen in nature as a mechanism for organismal adaptation and survival against harsh conditions. Legumes are well-known for possessing degradation-resistant proteins that often diminish their nutritional value. Here we applied diagonal two-dimensional (D2D) SDS-polyacrylamide gel electrophoresis (PAGE), a method that allows for the proteomics-level identification of KSPs, to a group of 12 legumes (mostly beans and peas) of agricultural and nutritional importance. Our proteomics results show beans that are more difficult to digest, such as soybean, lima beans, and various common beans, have high contents of KSPs. In contrast, mung bean, red lentil, and various peas that are highly digestible contain low amounts of KSPs. Identified proteins with high kinetic stability are associated with warm-season beans, which germinate at higher temperatures. In contrast, peas and red lentil, which are cool-season legumes, contain low levels of KSPs. Thus, our results show protein kinetic stability is an important factor in the digestibility of legume proteins and may relate to nutrition efficiency, timing of seed germination, and legume resistance to biotic stressors. Furthermore, we show D2D SDS-PAGE is a powerful method that could be applied for determining the abundance and identity of KSPs in engineered and wild legumes and for advancing basic research and associated applications.

The effects of water sample treatment, preparation, and storage prior to cyanotoxin analysis for cylindrospermopsin, microcystin and saxitoxin.

Cyanobacterial harmful algal blooms occur in freshwater lakes, ponds, rivers, and reservoirs, and in brackish waters throughout the world. The wide variety of cyanotoxins and their congeners can lead to frequent exposure of humans through consumption of meat, fish, seafood, blue-green algal products and water, accidental ingestion of contaminated water and cyanobacterial scum during recreational activities, and inhalation of cyanobacterial aerosols. Cyanotoxins can also occur in the drinking water supply. In order to monitor human exposure, sensitive analytical methods such as enzyme linked immunosorbent assay and liquid chromatography-mass spectrometry are often used. Regardless of the analytical method of choice, some problems regularly occur during sample collection, treatment, storage, and preparation which cause toxin loss and therefore underestimation of the true concentration. To evaluate the potential influence of sample treatment, storage and preparation materials on surface and drinking water samples, the effects of different types of materials on toxin recovery were compared. Collection and storage materials included glass and various types of plastics. It was found that microcystin congeners LA and LF adsorbed to polystyrene, polypropylene, high density polyethylene and polycarbonate storage containers, leading to low recoveries (<70%), cylindrospermopsin and saxitoxin did not adsorb to the containers tested. Therefore, this study shows that glass or polyethylene terephthalate glycol containers are the materials of choice for collection and storage of samples containing the cyanotoxins cylindrospermopsin, microcystins, and saxitoxin. This study also demonstrated that after 15 min chlorine decreased the concentration of microcystin LR to <40%, microcystin LA and saxitoxin to <15%, therefore quenching of drinking water samples immediately upon sample collection is critical for accurate analysis. In addition, the effect of various drinking water treatment chemicals on toxin recovery and the behavior of those chemicals in the enzyme linked immunosorbent assays were also studied and are summarized.

Measurement of triclosan in water using a magnetic particle enzyme immunoassay.

A sensitive magnetic particle-based immunoassay to determine triclosan [5-chloro-2-(2,4-dichlorophenoxy)phenol] in drinking water and wastewater was developed. Rabbit antiserum was produced by immunizing the rabbit with 6-[5-chloro-2-(2,4-dichlorophenoxy)phenoxy]hexanoic acid-keyhole limpet hemocyanin. Horseradish peroxidase was conjugated with 4-[3-bromo-4-(2,4-dibromophenoxy)phenoxy]butyric acid via N-hydroxysuccinimide (NHS) and 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC). The triclosan antibody was coupled to magnetic particles via the NHS/EDC reaction. The antibodies were able to recognize some structurally related polybrominated biphenyl ethers but did not recognize various common pollutants that were less similar to the hapten. The ELISA could detect triclosan in standard solution (25% methanol/H2O v/v) at 20 ppt and its metabolite, methyl-triclosan, at 15 ppt. Water samples from different treatment stages were prepared to contain 25% methanol and analyzed directly without any sample extraction or preconcentration. The results showed that recoveries were >80% and the % CV was <10%, demonstrating the assay was both accurate and precise. Application of the triclosan ELISA to water treatment plants showed that tap water at various purification stages had low concentrations of triclosan (<20 ppt) and required an increased sample size for appropriate detection and measurement. Application of ELISA to the wastewater treatment plants (WWTP) demonstrated high concentrations of triclosan (in general, >3000 ppt in water entering the WWTP) with the levels decreasing as the water proceeded through the processing plant (<500 ppt at outflow sewage). The ELISA measurement was shown to be equivalent to the more specific GC-MS analysis on a number of wastewater treatment samples with a high degree of correlation, with the exception of a few samples with very high triclosan concentrations (>5000 ppt). Measurement of methyl-triclosan (in WWTP) using GC-MS demonstrated the levels of this compound to be low. In summary, a rapid, sensitive, accurate, and precise magnetic particle-based immunoassay has been developed for triclosan analysis, which can serve as a cost-effective monitoring tool for various water samples.