128 research outputs found

    Is a Framework of Support Enough? Undergraduate Research for Online STEM Students

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    While undergraduate research is known as a high-impact practice, little research has been conducted for the online educational setting. Early research suggests that online students and faculty have similar interest in undergraduate research as their residential (face-to-face) counterparts. This point of view presents the framework of support developed for fully online students distributed globally and shares some of the challenges faced in online undergraduate research, including the issue of low recruitment (despite stated interest) that could be exacerbated by the COVID-19 pandemic

    Guiding Undergraduate Researchers in the Virtual World: Mentoring Experiences of Globally Distributed Students

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    The advancement of technology has led to an increase in undergraduate students pursuing degrees online. The translation of undergraduate research to the online environment is relatively new, though gaining momentum, partly due to the COVID-19 pandemic. Mentoring is a key undergraduate research support, particularly for those engaged online, as it fosters a supportive environment for online students to develop their skills and knowledge in their field of study. This study aims to explore the positive impacts of mentoring undergraduate research for fully online students. A single case study methodology was used, with interview data collected from four research mentees completing their degrees fully online. While this study is exploratory and further research with a larger sample size is necessary, the preliminary findings suggest that virtual mentoring can lead to a stronger sense of belonging, enhanced understanding of research processes, professional development (including career path and transferable skills), and continuous personal growth. These results highlight the importance of providing research mentoring opportunities to online students

    Manual pages for SAGA software tools, appendix H

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    Several pages from the SAGA UNIX programmer's manual are presented. These pages are for SAGA software tools

    Building Undergraduate Research in a Fully Online Engineering Program

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    This paper describes the creation and implementation of the support network of the Research Scholars Program at the Worldwide campus of Embry-Riddle Aeronautical University. Funded by an NSF IUSE grant, the purpose of this new program is to increase the opportunity for online engineering and engineering technology students to participate in undergraduate research. Studies have shown that participation in research can have an important impact on students, though online students are likely underrepresented in undergraduate research. The Research Scholars Program uses existing support systems of the campus while also building new components. These new components developed for this project are a research mentoring program, a workshop series, and a guided independent study course. The Research Scholars Program formalizes the process for online students at the Worldwide campus to participate in undergraduate research with a goal of having students publish and present their work

    Board 256: Development and Evolution of Workshops to Support Online Undergraduate Research

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    Under a National Science Foundation (NSF) Improving Undergraduate STEM Education (IUSE) grant, the Research Scholars Program was developed at Embry-Riddle Aeronautical University — Worldwide. The objective of the Research Scholars Program is to promote undergraduate research for the online students at the Worldwide campus and to formalize the process in which the students can participate in research. A significant aspect of the project was to create a support network for the students that incorporated existing services provided by the university and established new services to aid students throughout their mentored research experience. One of the new services was the development and delivery of starting in the second year of the grant and continuing through the third year. The purpose of the workshops is to introduce students to different aspects of research. The first series of workshops (offered in the 2021-2022 academic year) were mostly informational and provided initial support for undergraduate researchers. From the experience of developing and hosting the first series, the style of the second series (offered in the 2022-2023 academic year) was modified to try to promote more audience participation

    SAGA: A project to automate the management of software production systems

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    The SAGA system is a software environment that is designed to support most of the software development activities that occur in a software lifecycle. The system can be configured to support specific software development applications using given programming languages, tools, and methodologies. Meta-tools are provided to ease configuration. The SAGA system consists of a small number of software components that are adapted by the meta-tools into specific tools for use in the software development application. The modules are design so that the meta-tools can construct an environment which is both integrated and flexible. The SAGA project is documented in several papers which are presented

    Experimental phasing with SHELXC/D/E: combining chain tracing with density modification

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    Experimental phasing with SHELXC/D/E has been enhanced by the incorporation of main-chain tracing into the iterative density modification; this also provides a simple and effective way of exploiting noncrystallographic symmetry

    Geometric properties of nucleic acids with potential for autobuilding

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    Algorithms and geometrical properties are described for the automated building of nucleic acids in experimental electron density

    Analysis of nucleoside-binding proteins by ligand-specific elution from dye resin: application to Mycobacterium tuberculosis aldehyde dehydrogenases

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    We show that Cibacron Blue F3GA dye resin chromatography can be used to identify ligands that specifically interact with proteins from Mycobacterium tuberculosis, and that the identification of these ligands can facilitate structure determination by enhancing the quality of crystals. Four native Mtb proteins of the aldehyde dehydrogenase (ALDH) family were previously shown to be specifically eluted from a Cibacron Blue F3GA dye resin with nucleosides. In this study we characterized the nucleoside-binding specificity of one of these ALDH isozymes (recombinant Mtb Rv0223c) and compared these biochemical results with co-crystallization experiments with different Rv0223c-nucleoside pairings. We found that the strongly interacting ligands (NAD and NADH) aided formation of high-quality crystals, permitting solution of the first Mtb ALDH (Rv0223c) structure. Other nucleoside ligands (AMP, FAD, adenosine, GTP and NADP) exhibited weaker binding to Rv0223c, and produced co-crystals diffracting to lower resolution. Difference electron density maps based on crystals of Rv0223c with various nucleoside ligands show most share the binding site where the natural ligand NAD binds. From the high degree of similarity of sequence and structure compared to human mitochondrial ALDH-2 (BLAST Z-score = 53.5 and RMSD = 1.5 Å), Rv0223c appears to belong to the ALDH-2 class. An altered oligomerization domain in the Rv0223c structure seems to keep this protein as monomer whereas native human ALDH-2 is a multimer

    Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes

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    The yeast aminoacyl-tRNA synthetase (aaRS) complex is formed by the methionyl- and glutamyl-tRNA synthetases (MetRS and GluRS, respectively) and the tRNA aminoacylation cofactor Arc1p. It is considered an evolutionary intermediate between prokaryotic aaRS and the multi- aaRS complex found in higher eukaryotes. While a wealth of structural information is available on the enzymatic domains of single aaRS, insight into complex formation between eukaryotic aaRS and associated protein cofactors is missing. Here we report crystal structures of the binary complexes between the interacting domains of Arc1p and MetRS as well as those of Arc1p and GluRS at resolutions of 2.2 and 2.05 Å, respectively. The data provide a complete structural model for ternary complex formation between the interacting domains of MetRS, GluRS and Arc1p. The structures reveal that all three domains adopt a glutathione S-transferase (GST)-like fold and that simultaneous interaction of Arc1p with GluRS and MetRS is mediated by the use of a novel interface in addition to a classical GST dimerization interaction. The results demonstrate a novel role for this fold as a heteromerization domain specific to eukaryotic aaRS, associated proteins and protein translation elongation factors
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