Within scientific teams, a culture of community (the facilitation of shared values, goals, and an environment where individuals feel valued and want to engage in a team’s work) has implications for members’ learning and participation, and the team’s functioning, cohesion, and productivity. Drawing on 12 focus group interviews conducted over four years with 23 participants, we used an autoethnographic approach to examine how a research team developed a positive culture of community that influences its cohesion and productivity. We present six interconnected cultural practices that can foster a culture of community in settings where team-based learning and collaborations are required.
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Top-down proteomics by mass spectrometry (MS)
involves the mass measurement of an intact protein followed by subsequent
activation of the protein to generate product ions. Electron-based
fragmentation methods like electron capture dissociation (ECD) and electron
transfer dissociation (ETD) are widely used for these types of analysis,
however these fragmentation methods can be inefficient due to the low energy
electrons fragmenting the protein without the dissociation products; that is no
detection of fragments formed. Recently, electron ionization dissociation (EID),
which utilizes higher energy electrons (> 20 eV) has been shown to be more
efficient for top-down protein fragmentation compared to other electron-based
dissociation methods. Here we demonstrate that the use of EID enhances protein
fragmentation and subsequent detection of protein fragments. Protein product
ions can form by either single cleavage events, resulting in terminal fragments
containing the C-terminus or N-terminus of the protein, or by multiple cleavage
events to give rise to internal fragments that do not contain the C-terminus or
N-terminus of the protein. Conventionally, internal fragments have been
disregarded as reliable assignments of these fragments were limited. Here, we
demonstrate that internal fragments generated by EID can account for ~20-40% of
the mass spectral signals detected by top-down EID-MS experiments. By including
internal fragments, the extent of the protein sequence that can be explained
from a single tandem mass spectrum increases from ~50% to ~99% for 29 kDa
carbonic anhydrase II and 8.6 kDa ubiquitin. By including internal fragments in
the data analysis, previously unassigned peaks can be readily and accurately
assigned to enhance the efficiencies of top-down protein sequencing
experiments.
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