Dynamics differentiate between active and inactive inteins.

The balance between stability and dynamics for active enzymes can be somewhat quantified by studies of intein splicing and cleaving reactions. Inteins catalyze the ligation of flanking host exteins while excising themselves. The potential for applications led to engineering of a mini-intein splicing domain, where the homing endonuclease domain of the Mycobacterium tuberculosis RecA (Mtu recA) intein was removed.

Obstetric float nurse role redesign in a small rural community hospital.

Purpose: The purpose of this process improvement project in a rural community hospital with a small volume perinatal service was to foster a cooperative working environment between the obstetric and medical-surgical nursing teams and promote quality nursing care by evaluating, revising, and clearly defining the obstetric float nurse role.

Scope Of The Problem: Members of the obstetric and medical-surgical nursing team were convened to evaluate the obstetric float nurse role and develop plans for improvement. Nurses from both units participated in a written survey before and after the project was completed.

Preliminary exploration of the use of a medical malpractice self-study module.

This study was conducted to determine the effectiveness of an educational module on medical malpractice litigation and the use of evidence-based practice guidelines. Data regarding knowledge acquisition, ease of use, and the perceived value of the educational module were collected. A pretest-posttest design was used.

Characterization of recombinant human IL-15 deamidation and its practical elimination through substitution of asparagine 77.

Purpose: The use of recombinant human interleukin (rhIL)-15 as a potential therapeutic immune modulator and anticancer agent requires pure, stable preparations. However, purified rhIL-15 preparations readily accumulated heterogeneities. We sought to improve rhIL-15 stability through process, formulation, and targeted amino acid changes.

Purification and protective efficacy of monomeric and modified Yersinia pestis capsular F1-V antigen fusion proteins for vaccination against plague.

The F1-V vaccine antigen, protective against Yersinia pestis, exhibits a strong tendency to multimerize that affects larger-scale manufacture and characterization. In this work, the sole F1-V cysteine was replaced with serine by site-directed mutagenesis for characterization of F1-V non-covalent multimer interactions and protective potency without participation by disulfide-linkages. F1-V and F1-V(C424S) proteins were overexpressed in Escherichia coli, recovered using mechanical lysis/pH-modulation and purified from urea-solubilized soft inclusion bodies, using successive ion-exchange, ceramic hydroxyapatite, and size-exclusion chromatography.