Edith Holmes Met the Challenges to Lead to the Next Level.

After 19 years at the helm, we are privileged to honor Ms. Edith Holmes upon her retirement as Executive Director/Publisher of . Ms.

Utilization of Neurophysiological Classification Systems in Determining Interventions for Patients with Carpal Tunnel Syndrome.

Background: Median mononeuropathy at or distal to the wrist, or carpal tunnel syndrome (CTS), is the most common peripheral nerve compression disorder in the upper extremity. Neurophysiological classification systems for patients with CTS have been developed and implemented to provide health care providers an enhanced system of electrophysiological evaluation with a grading scale, so that they may evaluate their patients with CTS within a system that confers relative severity. Electrophysiological data collected within these classification systems includes either nerve conduction studies (NCS), or both NCS and electromyography (EMG) test results.

Illuminating Disorder Induced by Glu in a Stable Arg-Anchored Transmembrane Helix.

Membrane proteins are vital for biological function and are complex to study. Even in model peptide-lipid systems, the combined influence or interaction of pairs of chemical groups still is not well understood. Disordered proteins, whether in solution or near lipid membranes, are an emerging paradigm for the initiation and control of biological function.

Lipid-Dependent Titration of Glutamic Acid at a Bilayer Membrane Interface.

The ionization properties of protein side chains in lipid-bilayer membranes will differ from the canonical values of side chains exposed to an aqueous solution. While the propensities of positively charged side chains of His, Lys, and Arg to release a proton in lipid membranes have been rather well characterized, the propensity for a negatively charged Glu side chain to receive a proton and achieve the neutral state in a bilayer membrane has been less well characterized. Indeed, the ionization of the glutamic acid side chain has been predicted to depend on its depth of burial in a lipid membrane but has been difficult to verify experimentally.

Examination of pH dependency and orientation differences of membrane spanning alpha helices carrying a single or pair of buried histidine residues.

We have employed the peptide framework of GWALP23 (acetyl-GGALWLALALALALALALWLAGA-amide) to examine the orientation, dynamics and pH dependence of peptides having buried single or pairs of histidine residues. When residue L8 is substituted to yield GWALP23-H, acetyl-GGALWLAHALALALALALWLAGA-amide, the deuterium NMR spectra of H-labeled core alanine residues reveal a helix that occupies a single transmembrane orientation in DLPC, or in DMPC at low pH, yet shows multiple states at higher pH or in bilayers of DOPC. Moreover, a single histidine at position 8 or 16 in the GWALP23 framework is sensitive to pH.