MARC보기
LDR00000nmm u2200205 4500
001000000330785
00520241104161816
008181129s2018 ||| | | | eng d
020 ▼a 9780438125384
035 ▼a (MiAaPQ)AAI10902931
035 ▼a (MiAaPQ)umichrackham:001175
040 ▼a MiAaPQ ▼c MiAaPQ ▼d 248032
0491 ▼f DP
0820 ▼a 530
1001 ▼a Kamgar-Parsi, Kian.
24510 ▼a Amyloid Aggregation Behavior of Human Calcitonin.
260 ▼a [S.l.] : ▼b University of Michigan., ▼c 2018
260 1 ▼a Ann Arbor : ▼b ProQuest Dissertations & Theses, ▼c 2018
300 ▼a 141 p.
500 ▼a Source: Dissertation Abstracts International, Volume: 79-12(E), Section: B.
500 ▼a Adviser: Ayyalusamy Ramamoorthy.
5021 ▼a Thesis (Ph.D.)--University of Michigan, 2018.
520 ▼a 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
520 ▼a 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
520 ▼a 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
520 ▼a 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
590 ▼a School code: 0127.
650 4 ▼a Applied physics.
690 ▼a 0215
71020 ▼a University of Michigan. ▼b Applied Physics.
7730 ▼t Dissertation Abstracts International ▼g 79-12B(E).
773 ▼t Dissertation Abstract International
790 ▼a 0127
791 ▼a Ph.D.
792 ▼a 2018
793 ▼a English
85640 ▼u http://www.riss.kr/pdu/ddodLink.do?id=T15000442 ▼n KERIS
980 ▼a 201812 ▼f 2019
990 ▼a 관리자 ▼b 관리자