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https://d1y502jg6fpugt.cloudfront.net/17269/archive/files/1a2437e2bf313699ee4234f4348cb951.pdf?Expires=1712793600&Signature=do18u5vU0R0BtACIQbRqb4Od2AWXzMjbGkPIIvHJ-j1b4bWc4CzuIghdOmS7vHb-%7E93%7EaOhHd5iJdAJceJ1iXt7mrbUevgkPfrQaERiNKCFfm5aZzSmcUoz8mTrBOEiyNAUX5w8IXwlljSx9vdzfjWYBQGcEgjkkyFtSlSa0wdwROC7NOlpBz95j9aAv%7E5ARK8YmyqAXN5m-mNK0waYQ7YCdBwfz2ZEr6zbfEQs91Ra0odU3IeLF3y17epnv5DFBQIwl0AbNdcy7rqzRTmt%7EOiUWZ1x26m4FRfaRugrX-uQ45wkujuLzYHoSqGnj7vfv3zGVA9db2%7E4JPEF%7EzdvbPA__&Key-Pair-Id=K6UGZS9ZTDSZM
da235e0354078d4a05ee310d72489d53
Dublin Core
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Title
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Senior Showcase 2016
Description
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Oral and poster presentations from Senior Showcase held on April 19, 2016 at Ripon College.
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Ripon College Lane Library
Date
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April 2016
Contributor
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Ripon College Seniors 2016
Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
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Determination of Potential 4-hydroxy-2-nonenal Covalent Binding Sites on Electron Transfer Flavoprotein using Liquid Chromatography-Mass Spectrometry by Margaret Breen-Lyles
Subject
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Chemistry-Biology
Creator
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Breen-Lyles, Margaret
Source
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Senior Showcase Poster presentation
Publisher
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Ripon College
Date
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April 19, 2016
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Major: Chemistry-Biology
Minor: Spanish
Summer Research at Ripon College under Dr. Colleen Byron
Description
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Oxygen radicals and the reactive by-products they create have long been indicated in the disease pathways of metabolic disorders, given that they have the potential to react with the key components of proteins and thus disrupt their functioning. One of the most common by-products of oxygen radicals reacting with components of the cell is 4-hydroxy-2-nonenal (4HNE). Numerous studies have indicated that 4HNE is able to adduct to single amino acids, peptide sequences, as well as whole proteins. Electron transfer flavoprotein (ETF) is a highly active electron transferase of the fatty acid and amino acid oxidation pathways, and deficiency of this protein has been indicated in numerous disease pathways. ETF has demonstrated reduced activity when incubated with 4HNE, therefore this study attempted to determine possible binding sites of 4HNE on ETF by utilizing model peptides and LC-MS analysis. Distinct 4HNE adducts were formed with the peptide angiotensin II as well as a peptide from the alpha subunit of ETF. The groundwork has been laid for further research into the possibility of cross-linking occurring between ETF subunits as well as analysis of 4HNE adducts on ETF through tryptic digest.
Chemistry-Biology