자료유형 | 학위논문 |
---|---|
서명/저자사항 | Amyloid Aggregation Behavior of Human Calcitonin. |
개인저자 | Kamgar-Parsi, Kian. |
단체저자명 | University of Michigan. Applied Physics. |
발행사항 | [S.l.]: University of Michigan., 2018. |
발행사항 | Ann Arbor: ProQuest Dissertations & Theses, 2018. |
형태사항 | 141 p. |
기본자료 저록 | Dissertation Abstracts International 79-12B(E). Dissertation Abstract International |
ISBN | 9780438125384 |
학위논문주기 | Thesis (Ph.D.)--University of Michigan, 2018. |
일반주기 |
Source: Dissertation Abstracts International, Volume: 79-12(E), Section: B.
Adviser: Ayyalusamy Ramamoorthy. |
요약 | Under appropriate conditions, certain peptides and proteins, both intrinsically disordered and misfolded from their native state, can self-associate to form long proteinaceous fibrils known as amyloids. This transition forms the molecular basis |
요약 | A direct relationship between human calcitonin (hCT) concentration and aggregation lag time was observed for the first time, contrary to the conventional understanding of amyloid aggregation. This kinetic trend was found to persist over a range |
요약 | The determinants of hCT lag time were further investigated in a membrane environment, providing the first systematic study of the effect of membranes on CT aggregation. The direct relationship between peptide concentration and lag phase was foun |
요약 | The results of this thesis, particularly as they relate to monomer growth competence, represent significant contributions to the amyloid field and CT therapy. The novel kinetic mechanism proposed reveals that intramolecular interactions in disor |
일반주제명 | Applied physics. |
언어 | 영어 |
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: 이 자료의 원문은 한국교육학술정보원에서 제공합니다. |