Expanding faculty development through capacity-building: An institutional case study

The global pandemic highlighted the need for diverse faculty development partners to ensure student and faculty learning was supported, particularly in intensive modes of educational delivery. Our paper presents an institutional case study of how educational technology, in collaboration with the Center for Teaching and Learning and subject matter experts, served as untapped providers of faculty development. We detail the decision to shift to an intensive 7-week module system rather than our traditional 15-week semester in response to COVID-19. Although challenging for both faculty and students, this shift in educational delivery facilitated innovative approaches to faculty and student learning that are present on our campus today. This institutional case study highlights the role that capacity-building plays in capability development and professional learning for faculty and students alike to support effective teaching practice across diverse delivery modes

Systems Alignment for Comprehensive Faculty Development in Liberal Arts Colleges

Using an alignment framework, the authors explore faculty development initiatives in liberal arts colleges in order to understand the connection between organizational priorities and processes as connected to faculty members’ stated needs. The study draws on mixed methods data from The Initiative for Faculty Development in Liberal Arts Colleges (IFDLAC), including survey andinterview data from the 13 member institutions of the Great Lakes Colleges Association (GLCA).The authors offer future implications for faculty development practice

Rapid online buffer exchange for screening of proteins, protein complexes and cell lysates by native mass spectrometry

It is important to assess the identity and purity of proteins and protein complexes during and after protein purification to ensure that samples are of sufficient quality for further biochemical and structural characterization, as well as for use in consumer products, chemical processes and therapeutics. Native mass spectrometry (nMS) has become an important tool in protein analysis due to its ability to retain non-covalent interactions during measurements, making it possible to obtain protein structural information with high sensitivity and at high speed. Interferences from the presence of non-volatiles are typically alleviated by offline buffer exchange, which is time-consuming and difficult to automate. We provide a protocol for rapid online buffer exchange (OBE) nMS to directly screen structural features of pre-purified proteins, protein complexes or clarified cell lysates. In the liquid chromatography coupled to mass spectrometry (LC-MS) approach described in this protocol, samples in MS-incompatible conditions are injected onto a short size-exclusion chromatography column. Proteins and protein complexes are separated from small molecule non-volatile buffer components using an aqueous, non-denaturing mobile phase. Eluted proteins and protein complexes are detected by the mass spectrometer after electrospray ionization. Mass spectra can inform regarding protein sample purity and oligomerization, and additional tandem mass spectra can help to further obtain information on protein complex subunits. Information obtained by OBE nMS can be used for fast (<5 min) quality control and can further guide protein expression and purification optimization

Why Employees Do Bad Things: Moral Disengagement And Unethical Organizational Behavior

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/90243/1/j.1744-6570.2011.01237.x.pd

Rapid online buffer exchange for screening of proteins, protein complexes and cell lysates by native mass spectrometry

It is important to assess the identity and purity of proteins and protein complexes during and after protein purification to ensure that samples are of sufficient quality for further biochemical and structural characterization, as well as for use in consumer products, chemical processes and therapeutics. Native mass spectrometry (nMS) has become an important tool in protein analysis due to its ability to retain non-covalent interactions during measurements, making it possible to obtain protein structural information with high sensitivity and at high speed. Interferences from the presence of non-volatiles are typically alleviated by offline buffer exchange, which is time-consuming and difficult to automate. We provide a protocol for rapid online buffer exchange (OBE) nMS to directly screen structural features of pre-purified proteins, protein complexes or clarified cell lysates. In the liquid chromatography coupled to mass spectrometry (LC-MS) approach described in this protocol, samples in MS-incompatible conditions are injected onto a short size-exclusion chromatography column. Proteins and protein complexes are separated from small molecule non-volatile buffer components using an aqueous, non-denaturing mobile phase. Eluted proteins and protein complexes are detected by the mass spectrometer after electrospray ionization. Mass spectra can inform regarding protein sample purity and oligomerization, and additional tandem mass spectra can help to further obtain information on protein complex subunits. Information obtained by OBE nMS can be used for fast (<5 min) quality control and can further guide protein expression and purification optimization

De novo design of protein logic gates

The design of modular protein logic for regulating protein function at the posttranscriptional level is a challenge for synthetic biology. Here, we describe the design of two-input AND, OR, NAND, NOR, XNOR, and NOT gates built from de novo–designed proteins. These gates regulate the association of arbitrary protein units ranging from split enzymes to transcriptional machinery in vitro, in yeast and in primary human T cells, where they control the expression of the TIM3 gene related to T cell exhaustion. Designed binding interaction cooperativity, confirmed by native mass spectrometry, makes the gates largely insensitive to stoichiometric imbalances in the inputs, and the modularity of the approach enables ready extension to three-input OR, AND, and disjunctive normal form gates. The modularity and cooperativity of the control elements, coupled with the ability to de novo design an essentially unlimited number of protein components, should enable the design of sophisticated posttranslational control logic over a wide range of biological functions

Diversity in collaborative research communities: a multicultural, multidisciplinary thesis writing group in public health

Writing groups for doctoral students are generally agreed to provide valuable learning spaces for Ph.D. candidates. Here an academic developer and the eight members of a writing group formed in a Discipline of Public Health provide an account of their experiences of collaborating in a multicultural, multidisciplinary thesis writing group. We consider the benefits of belonging to such a group for Ph.D. students who are operating in a research climate in which disciplinary boundaries are blurring and where an increasing number of doctoral projects are interdisciplinary in nature; in which both academic staff and students come from enormously diverse cultural and language backgrounds; and in which teamwork, networking and collaboration are prized but not always proactively facilitated. We argue that doctoral writing groups comprising students from diverse cultural and disciplinary backgrounds can be of significant value for postgraduates who wish to collaborate on their own academic development to improve their research writing and communication skills; at the same time, such collaborative work effectively builds an inclusive, dynamic research community.Cally Guerin, Vicki Xafis, Diana V. Doda, Marianne H. Gillam, Allison J. Larg, Helene Luckner, Nasreen Jahan, Aris Widayati and Chuangzhou X

Submeter bathymetric mapping of volcanic and hydrothermal features on the East Pacific Rise crest at 9°50′N

Author Posting. © American Geophysical Union, 2007. This article is posted here by permission of American Geophysical Union for personal use, not for redistribution. The definitive version was published in Geochemistry Geophysics Geosystems 8 (2007): Q01006, doi:10.1029/2006GC001333.Recent advances in underwater vehicle navigation and sonar technology now permit detailed mapping of complex seafloor bathymetry found at mid-ocean ridge crests. Imagenex 881 (675 kHz) scanning sonar data collected during low-altitude (~5 m) surveys conducted with DSV Alvin were used to produce submeter resolution bathymetric maps of five hydrothermal vent areas at the East Pacific Rise (EPR) Ridge2000 Integrated Study Site (9°50′N, “bull's-eye”). Data were collected during 29 dives in 2004 and 2005 and were merged through a grid rectification technique to create high-resolution (0.5 m grid) composite maps. These are the first submeter bathymetric maps generated with a scanning sonar mounted on Alvin. The composite maps can be used to quantify the dimensions of meter-scale volcanic and hydrothermal features within the EPR axial summit trough (AST) including hydrothermal vent structures, lava pillars, collapse areas, the trough walls, and primary volcanic fissures. Existing Autonomous Benthic Explorer (ABE) bathymetry data (675 kHz scanning sonar) collected at this site provide the broader geologic context necessary to interpret the meter-scale features resolved in the composite maps. The grid rectification technique we employed can be used to optimize vehicle time by permitting the creation of high-resolution bathymetry maps from data collected during multiple, coordinated, short-duration surveys after primary dive objectives are met. This method can also be used to colocate future near-bottom sonar data sets within the high-resolution composite maps, enabling quantification of bathymetric changes associated with active volcanic, hydrothermal and tectonic processes.This work was supported by an NSF Ridge2000 fellowship to V.L.F. and a Woods Hole Oceanographic Institution fellowship supported by the W. Alan Clark Senior Scientist Chair (D.J.F.). Funding was also provided by the Censsis Engineering Research Center of the National Science Foundation under grant EEC-9986821. Support for field and laboratory studies was provided by the National Science Foundation under grants OCE-9819261 (D.J.F. and M.T.), OCE-0096468 (D.J.F. and T.S.), OCE-0328117 (SMC), OCE-0525863 (D.J.F. and S.A.S.), OCE-0112737 ATM-0427220 (L.L.W.), and OCE- 0327261 and OCE-0328117 (T.S.). Additional support was provided by The Edwin Link Foundation (J.C.K.)

How many human proteoforms are there?

Despite decades of accumulated knowledge about proteins and their post-translational modifications (PTMs), numerous questions remain regarding their molecular composition and biological function. One of the most fundamental queries is the extent to which the combinations of DNA-, RNA- and PTM-level variations explode the complexity of the human proteome. Here, we outline what we know from current databases and measurement strategies including mass spectrometry-based proteomics. In doing so, we examine prevailing notions about the number of modifications displayed on human proteins and how they combine to generate the protein diversity underlying health and disease. We frame central issues regarding determination of protein-level variation and PTMs, including some paradoxes present in the field today. We use this framework to assess existing data and to ask the question, "How many distinct primary structures of proteins (proteoforms) are created from the 20,300 human genes?" We also explore prospects for improving measurements to better regularize protein-level biology and efficiently associate PTMs to function and phenotype