Out with the old, in with the new: A reliable workflow in writing a report on diversity and inclusion

The Diversity Advisory Committee (DAC) will discuss the dynamics of the process of assessing the diversity health at the University of Maryland Libraries. From designing the survey instrument through analyzing the results to the final writing of the report of diversity and inclusion, the committee members will unveil their challenges and achievements in presenting unbiased conclusions from this assessment project. In completing this project, the committee consulted the university’s wisdom, including (1) the College of Information Studies for creating the survey; (2) the Office of Institutional Research, Planning and Assessment (IRPA), and Division of Information Technology (DIT) for analyzing the results; and (3) the Campus Assessment Working Group (CAWG) model for organizing the content of the final report.

Untangling Knots: Determining E-book Suitability for Course Reserves

E-books on their own are complex; they become even more so in the context of course reserves. In FY2016 the Resource Sharing & Reserves and Acquisitions units developed a new workflow for vetting requested e-books to ensure that they were suitable for course reserves (i.e. they permit unlimited simultaneous users) before posting links to them within the university’s online learning management system. In the Spring 2016 semester 46 e-books were vetted through this process, resulting in 18 purchases. Preliminary data analysis sheds light on the suitability of the Libraries’ current e-book collections for course reserves as well as faculty preferences, with potential implications for the Libraries’ ordering process. We hope this lightening talk will generate discussion about these issues among selectors, collection managers, and reserves staff alike.

Controlled Vocabulary Enhancement through Crowdsourcing: Project Andvari, Micropasts, and Public Quality Assurance

Proceedings paper published by Society of American Archivists. Presented at conference in 2015 in Cleveland, OH (http://www2.archivists.org/proceedings/research-forum/2015/agenda#papers). Published by SAA in 2016.

CHARACTERIZATION OF POLYUBIQUITIN CHAINS BY MASS SPECTROMETRY

The work outlined in this dissertation will allow biochemists and cellular biologists to characterize polyubiquitin chains involved in their cellular environment by following a facile mass spectrometric based workflow. The characterization of polyubiquitin chains has been of interest since their discovery in 1984. The profound effects of ubiquitination on the movement and processing of cellular proteins depend exclusively on the structures of mono and polyubiquitin modifications anchored or unanchored on the protein within the cellular environment. However, structure-function studies have been hindered by the difficulty in identifying complex chain structures due to limited instrument capabilities of the past. Genetic mutations or reiterative immunoprecipitations have been used previously to characterize the polyubiquitin chains, but their tedium makes it difficult to study a broad ubiquitinome. Top-down and middle-out mass spectral based proteomic studies have been reported for polyubiquitin and have had success in characterizing parts of the chain, but no method to date has been successful at differentiating all theoretical ubiquitin chain isomers (ubiquitin chain lengths from dimer to tetramer alone have 1340 possible isomers). The workflow presented here can identify chain length, topology and linkages present using a chromatographic-time-scale compatible, LC-MS/MS based workflow. To accomplish this feat, the strategy had to exploit the most recent advances in top-down mass spectrometry. This included the most advanced electron transfer dissociation (ETD) activation and sensitivity for large masses from the orbitrap Fusion Lumos. The spectral interpretation had to be done manually with the aid of a graphical interface to assign mass shifts because of a lack of software capable to interpret fragmentation across isopeptide linkages. However, the method outlined can be applied to any mass spectral based system granted it results in extensive fragmentation across the polyubiquitin chain; making this method adaptable to future advances in the field.