Teaching concepts of transesophageal echocardiography via Web-based modules.

OBJECTIVES: Teaching transesophageal echocardiography (TEE) remains challenging. The authors hypothesized that using online modules with live teaching in an echo training course would be feasible and result in superior knowledge acquisition to live teaching only. DESIGN: In this prospective cohort study, the authors implemented a TEE course with online modules and live teaching and compared it to a live-teaching-only version. SETTING: The online-and-live-teaching version of the course consisted of online modules and live sessions at Beth Israel Deaconess Medical Center (BIDMC), an academic medical center. The live-teaching-only version consisted of live sessions at BIDMC. PARTICIPANTS: Course participants included anesthesia trainees at BIDMC. INTERVENTIONS: Trainees taking the online-and-live-teaching version viewed online modules before live review lectures and simulation. Trainees taking the live-teaching-only version viewed live lectures before simulation. MEASUREMENTS AND MAIN RESULTS: Twenty-seven trainees completed the online-and-live-teaching version; six completed the live-teaching-only version. Trainees took a course exam after the first and last live sessions. For the online-and-live-teaching version, average pretest and posttest scores were 62.0%±13.7% and 77.5%±8.1%, respectively; pretest and posttest passing (≥70%) rates were 29.6% and 85.2%, respectively. Compared to the live-teaching-only version, the average pretest score was not significantly different (p=0.17), but the average posttest score was significantly higher (p=0.01). Trainee comfort with, and knowledge of, TEE increased after both versions. Trainees rated the utility of the live lectures and online modules similarly. CONCLUSIONS: A multimodal TEE curriculum increased trainees' knowledge of TEE concepts and had a positive reception from trainees.

Structure of the EntB multidomain nonribosomal peptide synthetase and functional analysis of its interaction with the EntE adenylation domain.

Nonribosomal peptide synthetases are modular proteins that operate in an assembly line fashion to bind, modify, and link amino acids. In the E. coli enterobactin NRPS system, the EntE adenylation domain catalyzes the transfer of a molecule of 2,3-dihydroxybenzoic acid to the pantetheine cofactor of EntB. We present here the crystal structure of the EntB protein that contains an N-terminal isochorismate lyase domain that functions in the synthesis of 2,3-dihydroxybenzoate and a C-terminal carrier protein domain. Functional analysis showed that the EntB-EntE interaction was surprisingly tolerant of a number of point mutations on the surface of EntB and EntE. Mutational studies on EntE support our previous hypothesis that members of the adenylate-forming family of enzymes adopt two distinct conformations to catalyze the two-step reactions.