1
15
3
-
https://d1y502jg6fpugt.cloudfront.net/17269/archive/files/1df46afbdc690f1eaf5d830df2b23df4.pdf?Expires=1712793600&Signature=LKlLBAs-ZTswkLhRAHe-Ze%7E%7EvIlK0SFmoCXd2SqbgEwuwzyQqQ0EQwkNolMxTmfdAXEPIOXOSJ5Q3%7Et%7EK%7EdpCslupn42Q28z8woUKvYX%7E9YsCTYa1CGjZuLMxxVGOORU8YOJSYfAhxjoPkguto4Pt3DKTTAY2Z-4vrjrbVKh-Nhf5YUhtute5BW7bLThOmnUhvEcK1LvPnL%7EuAcXYw2UIe7UgFWt9QKNWsCC7tcQh-sUzIeR39OxecjKHRqAfnHEghyuEzwe%7E3VY2EYfW3ZgSYxtAonpIOEZazSYltJDj5qc%7EydmmIR%7E8352tNSh0k1GuO2qQqJIlMmonNrSZsPJDg__&Key-Pair-Id=K6UGZS9ZTDSZM
2bba79dd1c6e3df18f78ab1c7fb5ce7a
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
A name given to the resource
Senior Showcase 2018
Description
An account of the resource
Oral and poster presentations from Senior Showcase held on April 17, 2018 at Ripon College.
Publisher
An entity responsible for making the resource available
Ripon College Lane Library
Date
A point or period of time associated with an event in the lifecycle of the resource
April 17, 2018
Contributor
An entity responsible for making contributions to the resource
Ripon College Seniors 2018
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
A name given to the resource
Predatory Bacteria: Investigating the Role of Lipopolysaccharides and opmA Mutations on Predation by Isaac Masters
Subject
The topic of the resource
Biology
Creator
An entity primarily responsible for making the resource
Isaac Masters
Source
A related resource from which the described resource is derived
Senior Showcase Poster presentation
Publisher
An entity responsible for making the resource available
Ripon College
Date
A point or period of time associated with an event in the lifecycle of the resource
April 17, 2018
Rights
Information about rights held in and over the resource
The author reserves all rights.
Format
The file format, physical medium, or dimensions of the resource
pdf
Identifier
An unambiguous reference to the resource within a given context
Major: Chemistry-Biology
Greenfield, Illinois
BIO 502: Biology Senior Seminar
Description
An account of the resource
In recent years, there have been studies that evaluate the potential use of predatory bacteria Bdellovibrio bacteriovorus to control the multidrug-resistant (MDR), Gram-negative pathogens associated with human infections. This study was focused on analyzing various Lipopolysaccharide and outer membrane protein mutants of forty Acinetobacter baumannii mutants in order to evaluate which factors play a role in predation. Although most of the cycle of the Bdellovibrio is known, it is still relatively unknown how these predatory bacteria attach to its prey. By co-culturing Bdellovibrio bacteriovorus 109J with a model MDR organism, Acinetobacter baumannii, we were able to identify and examine specific mutations that result in decreased predation of the predatory bacteria on the model organism. Acinetobacter baumannii with an outer membrane protein (OMP) mutation on OmpA showed a decrease in predation after 24h. Additional experiments were done on one OmpA mutated Escherichia coli and three Pseudomonas aeruginosa strains but no significant effect was found. We have established that Bdellovibrio bacteriovorus reduced the amount of MDR Acinetobacter baumannii similarly in all mutants except outer membrane protein A. This research indicates that the attachment mechanism of Bdellovibrio bacteriovorus to Acinetobacter baumannii might play a vital role in predation. With the help of future studies, the proceeding steps would be to analyze the methodology further in order to solidify if outer membrane proteins play a role in attachment.
Acinetobacter baumannii
Bdellovibrio bacteriovorus
Chemistry-Biology
multidrug resistant pathogens
OmpA mutant
predatory bacteria
-
https://d1y502jg6fpugt.cloudfront.net/17269/archive/files/4db293db8061ff9f761e38af71cb89c4.pdf?Expires=1712793600&Signature=cf6GIbnwE7yYX6EmlFQYVR-wQdvqq4XHZeHo0kP7y90ngsALqwLec0YfvEycPx9GLNbs66jSwfa01DaaV14B9A9NRfVPekn7CT5hYVfjhtLwArcOeYq9UpzMgPyhLwnw4L2mfoOnZmdTmOlEUGgWGBOkLSXzMxvDz8O8QgMU4l077W56tFK4HmViL90jndmiwEd-beirewm7v3dp8n3PjTGCrRvnla8sa7lpj-1HjiHvGoTWq-KTMs85NxXCxmZqX2kfr-rkeg0BUWgtkV13-I8lFJ-NLmqDvy3YwaO4YSBODzkK5yOmKxAeBw%7EKKJ166gm4bcMZQKWZ4rNe3Zqmwg__&Key-Pair-Id=K6UGZS9ZTDSZM
e44c8016e9a4b5e19e90ea8e3692a31a
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
A name given to the resource
Senior Showcase 2017
Description
An account of the resource
Oral and poster presentations from Senior Showcase held on April 18, 2017 at Ripon College.
Publisher
An entity responsible for making the resource available
Ripon College Lane Library
Contributor
An entity responsible for making contributions to the resource
Ripon College Seniors 2017
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
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
A name given to the resource
Pondering Polyhelical Proteins: Mathematically Modeling Helical Repeat Proteins by Lincoln Wurtz
Subject
The topic of the resource
Mathematics
Creator
An entity primarily responsible for making the resource
Lincoln Wurtz
Source
A related resource from which the described resource is derived
Senior Showcase Oral Presentation
Publisher
An entity responsible for making the resource available
Ripon College
Date
A point or period of time associated with an event in the lifecycle of the resource
April 18, 2017
Rights
Information about rights held in and over the resource
The author reserves all rights.
Identifier
An unambiguous reference to the resource within a given context
Majors: Mathematics and Chemistry-Biology
Description
An account of the resource
Proteins are the most abundant biological macromolecules and, based on their
three-dimensional shape, perform life-sustaining functions. The process by which a
protein assumes its folded shape remains an open question and has intrigued biologist and chemists for decades. Mathematicians have joined forces with the natural scientists and brought with them the tools of differential geometry, which prove powerful for modeling proteins. We explore the method of [3] to model a small subset of proteins using polyhelical space curves. We successfully modeled three alpha-helical repeat proteins. The developed model has demonstrated possible uses in predicting theoretical tertiary structures of proteins given a set of secondary structures--a step in the right direction of solving the protein folding problem. Additionally, we provide insight into the relationship between clashes and the model's stability calculator, which may improve the viability of their model.
Chemistry-Biology
differential geometry
Mathematics
Protein
-
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
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
A name given to the resource
Senior Showcase 2016
Description
An account of the resource
Oral and poster presentations from Senior Showcase held on April 19, 2016 at Ripon College.
Publisher
An entity responsible for making the resource available
Ripon College Lane Library
Date
A point or period of time associated with an event in the lifecycle of the resource
April 2016
Contributor
An entity responsible for making contributions to the resource
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
A name given to the resource
Determination of Potential 4-hydroxy-2-nonenal Covalent Binding Sites on Electron Transfer Flavoprotein using Liquid Chromatography-Mass Spectrometry by Margaret Breen-Lyles
Subject
The topic of the resource
Chemistry-Biology
Creator
An entity primarily responsible for making the resource
Breen-Lyles, Margaret
Source
A related resource from which the described resource is derived
Senior Showcase Poster presentation
Publisher
An entity responsible for making the resource available
Ripon College
Date
A point or period of time associated with an event in the lifecycle of the resource
April 19, 2016
Rights
Information about rights held in and over the resource
The author reserves all rights.
Identifier
An unambiguous reference to the resource within a given context
Major: Chemistry-Biology
Minor: Spanish
Summer Research at Ripon College under Dr. Colleen Byron
Description
An account of the resource
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