Why do Latino Survey Respondents Acquiesce? Respondent and Interviewer Characteristics as Determinants of Cultural Patterns of Acquiescence among Latino Survey Respondents.

Research indicates that Latino survey respondents are more likely to acquiesce than non-Latino European Americans, thereby decreasing the potential for measurement invariance across cultural groups. In order to better understand what drives this culturally patterned response style, we examined the influence of respondent and interviewer characteristics on acquiescence. Data were obtained from a telephone survey of 400 Mexican American, Puerto Rican, Cuban American, and non-Latino European American respondents and a self-administered survey of 21 interviewers. Higher acquiescence was associated with several respondent characteristics: older age, lower education, stronger Latino cultural orientation, Spanish use, Latino ethnicity, and, among Latinos, Cuban American ethnicity. In contrast, acquiescence was not influenced by respondent-interviewer social distance, social deference, or interviewer characteristics (e.g., education, gender, acculturation, interviewer experience). These findings indicate that acquiescence differs across Latino ethnic subgroups and that respondent and language factors are more influential determinants of acquiescence than survey interviewers.

Enhanced enzyme stability through site-directed covalent immobilization.

Breakthroughs in enzyme immobilization have enabled increased enzyme recovery and reusability, leading to significant decreases in the cost of enzyme use and fueling biocatalysis growth. However, current enzyme immobilization techniques suffer from leaching, enzyme stability, and recoverability and reusability issues. Moreover, these techniques lack the ability to control the orientation of the immobilized enzymes. To determine the impact of orientation on covalently immobilized enzyme activity and stability, we apply our PRECISE (Protein Residue-Explicit Covalent Immobilization for Stability Enhancement) system to a model enzyme, T4 lysozyme. The PRECISE system uses non-canonical amino acid incorporation and the Huisgen 1,3-dipolar cycloaddition "click" reaction to enable directed enzyme immobilization at rationally chosen residues throughout an enzyme. Unlike previous site-specific systems, the PRECISE system is a truly covalent immobilization method. Utilizing this system, enzymes immobilized at proximate and distant locations from the active site were tested for activity and stability under denaturing conditions. Our results demonstrate that orientation control of covalently immobilized enzymes can provide activity and stability benefits exceeding that of traditional random covalent immobilization techniques. PRECISE immobilized enzymes were 50 and 73% more active than randomly immobilized enzymes after harsh freeze-thaw and chemical denaturant treatments.

Dynamical feature extraction at the sensory periphery guides chemotaxis.

Behavioral strategies employed for chemotaxis have been described across phyla, but the sensorimotor basis of this phenomenon has seldom been studied in naturalistic contexts. Here, we examine how signals experienced during free olfactory behaviors are processed by first-order olfactory sensory neurons (OSNs) of the Drosophila larva. We find that OSNs can act as differentiators that transiently normalize stimulus intensity-a property potentially derived from a combination of integral feedback and feed-forward regulation of olfactory transduction. In olfactory virtual reality experiments, we report that high activity levels of the OSN suppress turning, whereas low activity levels facilitate turning. Using a generalized linear model, we explain how peripheral encoding of olfactory stimuli modulates the probability of switching from a run to a turn. Our work clarifies the link between computations carried out at the sensory periphery and action selection underlying navigation in odor gradients.

Lyophilized Escherichia coli-based cell-free systems for robust, high-density, long-term storage.

Cell-free protein synthesis (CFPS) is a versatile tool for rapid recombinant protein production and engineering. One drawback of cell-free technology is the necessity to store the major components-cell extracts and energy systems-below freezing in bulky aqueous solutions. Here we describe simple methods for lyophilizing extracts and preparing powdered energy systems for CFPS. These techniques allow for high-density storage of cell-free systems that are more robust against temperature and bacterial degradation. Our methods have the potential to decrease storage expenses, allow for longer shelf-life of cell extracts at room temperature, and enable durable portable protein production technologies.

Reversed-phase membrane inlet mass spectrometry applied to the real-time monitoring of low molecular weight alcohols in chloroform.

Reversed-phase membrane inlet mass spectrometry incorporating a hollow-fiber Nafion membrane has been evaluated for the determination of low molecular weight alcohols in chloroform. The hydrophilic Nafion membrane preferentially transports methanol and ethanol, allowing percentage concentrations of the alcohols to be determined in a chloroform matrix. A linear response was observed for ethanol over the working range 0.5-2.5%, with a limit of detection of 0.1%. The application of reversed-phase membrane inlet mass spectrometry using a Nafion membrane to the monitoring of a chloroform recovery process has been investigated using a residual gas analyzer. Evolving methanol and ethanol concentrations were determined in real time and compared favorably with off-line determinations by gas chromatography.