Behavioral Responses of Nymph and Adult Cimex lectularius (Hemiptera: Cimicidae) to Colored Harborages.

Behavioral bioassays were conducted to determine whether bed bug adults and nymphs prefer specific colored harborages. Two-choice and seven-choice behavioral color assays indicate that red (28.5%) and black (23.

A low-E magic angle spinning probe for biological solid state NMR at 750 MHz.

Crossed-coil NMR probes are a useful tool for reducing sample heating for biological solid state NMR. In a crossed-coil probe, the higher frequency (1)H field, which is the primary source of sample heating in conventional probes, is produced by a separate low-inductance resonator. Because a smaller driving voltage is required, the electric field across the sample and the resultant heating is reduced.

The helical structure of surfactant peptide KL4 when bound to POPC: POPG lipid vesicles.

KL 4 is a 21-residue peptide employed as a functional mimic of lung surfactant protein B, which successfully lowers surface tension in the alveoli. A mechanistic understanding of how KL 4 affects lipid properties has proven elusive as the secondary structure of KL 4 in lipid preparations has not been determined at high resolution. The sequence of KL 4 is based on the C-terminus of SP-B, a naturally occurring helical protein that binds to lipid interfaces.

Determination of peptide backbone torsion angles using double-quantum dipolar recoupling solid-state NMR spectroscopy.

Several approaches for utilizing dipolar recoupling solid-state NMR (ssNMR) techniques to determine local structure at high resolution in peptides and proteins have been developed. However, many of these techniques measure only one torsion angle or are accurate for only certain classes of secondary structure. Additionally, the efficiency with which these dipolar recoupling experiments suppress the deleterious effects of chemical shift anisotropy (CSA) at high magnetic field strengths varies.

Optimizing ssNMR experiments for dilute proteins in heterogeneous mixtures at high magnetic fields.

Solid-state NMR spectroscopy at high magnetic fields is proving to be an effective technique in structural biology, particularly for proteins which are not amenable to traditional X-ray and solution NMR approaches. Several parameters can be selected to provide optimal sensitivity, improve sample stability, and ensure biological relevance for ssNMR measurements on protein samples. These include selection of sample conditions, NMR probe design, and design of pulse experiments.