Charge Pairs and Mutations in Collagen Mimetic Peptides

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dc.contributor.advisorHartgerink, Jeffrey D.en_US
dc.creatorClements, Katherine Annen_US
dc.date.accessioned2017-08-01T17:36:51Zen_US
dc.date.available2017-08-01T17:36:51Zen_US
dc.date.created2017-05en_US
dc.date.issued2017-04-10en_US
dc.date.submittedMay 2017en_US
dc.date.updated2017-08-01T17:36:51Zen_US
dc.description.abstractThis thesis will present insights into natural type I collagen based upon studies with collagen mimetic peptides. Natural collagen is a fibrous protein with challenging properties, such as solubility, which makes it difficult to study through analytical methods such as nuclear magnetic resonance spectroscopy. Collagen mimetic peptides are a flexible and controlled model system that imitates natural type I collagen structure, a triple helix, on a smaller scale, from over 1000 amino acids to around 30 amino acids. Chapter one will explore the development of collagen mimetic peptides and review the current design principle to form composition and register specific triple helices. Chapter two will illustrate the power of charge pairing in the triple helix with the creation of a triple helix with an extended offset through axial charge pairing. This is the first triple helix with an extended offset, proving that the offset triple helix is possible, even when it is not incorporated into a fiber. Chapters three and four will model mutations from Osteogenesis Imperfecta, a type I collagen disease, in collagen mimetic peptides. Osteogenesis Imperfecta results from mutations of the requisite glycines in the Xaa-Yaa-Gly repeat of collagen. Mutations in both the A and B chains of an AAB triple helix will be created, and their impact on the composition, stability, and structure of the triple helix will be examined through circular dichroism and nuclear magnetic resonance experiments. The results of those experiments will be used to create molecular models of the mutated triple helices. This series of studies gives insight into the forces in the triple helix: the destabilizing force of a mutation, the stabilizing force of hydrogen bonds, and the stabilizing, yet constricting, force of axial charge pairs. In these model systems, the mutation was able to direct the composition and register of the triple helix, where the triple helix with the lowest number of mutations would fold, even if it is not the most stabilized via charge pairing.en_US
dc.format.mimetypeapplication/pdfen_US
dc.identifier.citationClements, Katherine Ann. "Charge Pairs and Mutations in Collagen Mimetic Peptides." (2017) Diss., Rice University. <a href="https://hdl.handle.net/1911/96065">https://hdl.handle.net/1911/96065</a>.en_US
dc.identifier.urihttps://hdl.handle.net/1911/96065en_US
dc.language.isoengen_US
dc.rightsCopyright is held by the author, unless otherwise indicated. Permission to reuse, publish, or reproduce the work beyond the bounds of fair use or other exemptions to copyright law must be obtained from the copyright holder.en_US
dc.subjectcollagenen_US
dc.titleCharge Pairs and Mutations in Collagen Mimetic Peptidesen_US
dc.typeThesisen_US
dc.type.materialTexten_US
thesis.degree.departmentChemistryen_US
thesis.degree.disciplineNatural Sciencesen_US
thesis.degree.grantorRice Universityen_US
thesis.degree.levelDoctoralen_US
thesis.degree.nameDoctor of Philosophyen_US
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