ABSTRACT
This paper reports on an evaluation of a new concept in clinical nurse education: the Dedicated Education Unit (DEU). Developed by the School of Nursing, The Flinders University of South Australia, the DEU aims to optimise undergraduate student learning through enhancement of the clinical learning environment and collaboration between clinicians, academics and students. Three DEUs involving 91 students were evaluated, using primarily summative methods to elicit positive and negative attributes of the DEUs. Outcomes indicated that the DEU is a highly appropriate clinical placement model. (Part one of this paper explained the rationale for the DEU and its key features.)
Subject(s)
Academic Medical Centers/organization & administration , Education, Nursing, Baccalaureate/organization & administration , Hospital Units , Humans , Nursing Evaluation Research , South AustraliaABSTRACT
The Dedicated Education Unit (DEU) is a new concept in clinical nurse education. The DEU plays a major role in enhancing links between health care providers and The Flinders University of South Australia (FUSA) School of Nursing. This collaborative venture has created a more positive clinical learning environment, maximized the achievement of student learning outcomes, and nurtured closer partnership between clinicians and academics. Recognition of mutuality, respect and trust among all stakeholders is central to its success. This paper (part one) explains the rationale for the DEU and describes its inherent values. Part two reports on an evaluation of the DEU.
Subject(s)
Academic Medical Centers/organization & administration , Education, Nursing, Baccalaureate/organization & administration , Hospital Units , Students, Nursing/psychology , Humans , Nursing Education ResearchABSTRACT
Crystallographic studies play a major role in current efforts towards protein structure determination. However, despite recent advances in computational tools for molecular modeling and graphics, the task of constructing a model of the tertiary structure of a protein from experimental data remains complex and time-consuming, requiring extensive expert intervention. This paper describes an approach to protein model determination that incorporates crystallographic data, along with sequence data. A model is represented as an annotated graph that traces the backbone and side chains for a protein. The proposed approach incorporates numerical techniques that are applied to construct and analyze an electron density map for a unit cell of a crystal. The purpose of this work is to advance the ability to discern meaningful features of protein structure through the use of topological analysis of the relative density. Experimental results, which demonstrate the viability of the approach, are reported.