Showing 31 - 40 of 67 Items

Date: 2024-01-01
Creator: Devin Kathleen O’Loughlin
Access: Access restricted to the Bowdoin Community
Date: 2024-01-01
Creator: Ayanna S Hatton
Access: Open access
- When photons from sunlight are absorbed by plants, they can take paths of photosynthesis, fluorescence, or energy dissipation. Instruments to quantify fluorescence have expanded in scale to allow measurements from satellites and flux towers using Solar-Induced Chlorophyll Fluorescence (SIF). Studies have found a positive correlation between SIF and gross primary productivity (GPP; representative of photosynthesis), suggesting SIF is a proxy for GPP. This conclusion encourages the use of SIF to inform decisions about carbon budgets and responding to climate change. Studies of fluorescence on the single-leaf scale have revealed that SIF measurements do not account for all variables nor is there an understanding of the impact of environmental factors, such as drought, on these measurements. In this project, tall fescue turfgrass was placed in one of four differing drought severities for 19 days. Leaf-level measurements of photosynthesis and pulse-amplitude modulated fluorescence were made, demonstrating stomatal closure and inhibition of photosynthesis. This physiological change caused greater photon allocation to energy dissipation. Changes in greenness and the utilization of photoprotective mechanisms such as senescence and anthocyanin accumulation were observed. This study has provided an understanding of the temporal, physiological, and visible impacts of drought on turfgrass to inform interpretations of SIF in future experiments. Caution is crucial in utilizing SIF as a proxy for GPP before further research into the impact of drought on SIF is completed.

Date: 2024-01-01
Creator: William Joseph Surks
Access: Access restricted to the Bowdoin Community

- Embargo End Date: 2025-05-14
Date: 2020-01-01
Creator: Zachary C. LeBlanc
Access: Embargoed

Date: 2021-01-01
Creator: Andrew James Mulholland
Access: Access restricted to the Bowdoin Community

- Restriction End Date: 2025-06-01
Date: 2020-01-01
Creator: Rebecca Londoner
Access: Access restricted to the Bowdoin Community
Date: 2020-01-01
Creator: Edward Myron Bull
Access: Open access
- Neuropeptides are a class of small peptides that govern various neurological functions, and the American lobster (Homarus americanus) provides a model system for their characterization. Neuropeptides are commonly post-translationally modified (PTM), and one common PTM is glycosylation. Past research in the Stemmler lab has found glycosylated neuropeptides in H. americanus; however, the extent and biological role of this modification has not been well characterized. This study was undertaken to determine the number of glycosylated peptides in the sinus glands of H. americanus and to develop an approach to tag the site of glycosylation using beta-elimination chemistry. LC-MS paired with high pH reverse phase fractionation was used to survey for glycosylated neuropeptides and beta elimination with an amine tag was used as an approach to characterize the site of glycosylation. Our results indicate that high pH fractionation is a useful approach to simplify complex mixtures of neuropeptides and improve glycopeptide detection. Efforts to use beta elimination and tagging to characterize glycosylated neuropeptides have been less successful. Beta elimination of full length peptides resulted in peptide degradation. An approach utilizing chymotrypsin to reduce peptide size coupled with beta elimination and labeling with 2-dimethylaminoethanethiol showed less evidence for degradation, and this approach yielded data isolating two potential serine residues for the site of glycosylation; however, the data was not sufficient to distinguish the two sites. Work to optimize reaction conditions using a glycopeptide standard showed that multiple isomeric products were formed during beta elimination. With the goal of optimizing reaction conditions, future work will further examine reaction kinetics to eventually apply the approach to the entire sinus gland

Date: 2023-01-01
Creator: Emma Straw Noel
Access: Access restricted to the Bowdoin Community
Date: 2021-01-01
Creator: Ruby Chimereucheya Ahaiwe
Access: Open access
- The American lobster Homarus americanus uses its innate immune system for protection against foreign bodies and diseases. Hemocytes in the innate immune system are responsible for the rapid and effective cellular response against pathogens and infections observed in lobsters. These hemocytes, particularly semi-granulocytes and granulocytes, store antimicrobial peptides (AMPs) which specifically target and destroy microbes. Hemocyte samples from the American lobster Homarus americanus hemolymph or circulatory fluid, mixed and fractionated into separated semi-granular and granular cell samples, were analyzed for possible AMP presence. A defensin AMP, Hoa-D1, (SYVRSCSSNGGDCVYRCYGNIINGACSGSRVCCRSGGGYamide; with C representing a cysteine participating in a disulfide bond) was successfully isolated and identified by mass using reversed-phase high-performance liquid chromatography (HPLC) and liquid chromatography-mass spectrometry (LC-MS/MS). Preliminary results also show the defensin AMP to be concentrated in the semi-granulocytes and granulocytes.Hoa-D1 was isolated via HPLC fractionation. Isolated Hoa-D1 and semi-granular and granular hemocyte extracts were tested for bioactivity against the gram-negative bacteria, Escherichia coli, using the Kirby-Bauer disk diffusion assay. The assay did not show any activity, an outcome attributed to concentrations of the AMP that were too low to have any antimicrobial effect on E. coli. Subsequent work on this study should involve increasing the concentration of Hoa-D1 in test samples. Studying function of AMPs in the American lobster can provide more information on the depth of their cellular immune responses in other crustaceans, and possibly contribute to the development of novel antibiotics for treating diseases in humans.

Date: 2024-01-01
Creator: Foje-Geh Robert Tendoh
Access: Access restricted to the Bowdoin Community