Please use this identifier to cite or link to this item:
https://hdl.handle.net/10356/48015
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Zhang, Yu | en |
dc.date.accessioned | 2012-02-14T00:56:48Z | en |
dc.date.available | 2012-02-14T00:56:48Z | en |
dc.date.copyright | 2011 | en |
dc.date.issued | 2011 | en |
dc.identifier.citation | Zhang, Y. (2011). Mutagenesis studies to determine the key interfacial amino acid residues that govern the self-assembly of the ferritin protein cages. Doctoral thesis, Nanyang Technological University, Singapore. | en |
dc.identifier.uri | https://hdl.handle.net/10356/48015 | en |
dc.description.abstract | Investigations into protein quaternary structure can lead to deeper insight into the fundamentals governing both protein folding and protein-protein interactions. In addition they can provide a foundation for the eventual rational design of novel complex protein architectures. A maxi-ferritin, bacterioferritin from E. coli (BFR), and a mini-ferritin, DNA-binding protein from starved cells (DPS), despite their similar four-helix bundle tertiary structure, assemble into quaternary structure with different symmetries, octahedral and tetrahedral and oligomerization states, 24-mer and 12-mer, respectively. To understand how these two structurally analogous proteins assemble into nano-structures with different sizes and shapes, both proteins were chosen as the basis for a mutagenesis study to investigate the importance of key amino acid residues, located at symmetry-related protein-protein interfaces, in controlling protein stability and self-assembly. Several mutants were designed for each protein through simple inspection and computational analysis, synthesized and subjected to different chemical and biophysical methods to determine their thermal stability, self-assemble ability and structure. The data indicate that many of these residues may be hot spot residues. Several mutants were observed to completely shut down detectable solution formation of 24-mer, favoring a cooperatively folded dimer, suggesting that they may be oligomerization “switch residues”. This investigation into the structure and energetics of these self-assembling nano-cage proteins not only can act as a jumping off point for the eventual design of novel protein nano-structures and their applications, but it can also help to understand the role that structure plays in the function of these important classes of proteins. | en |
dc.format.extent | 191 p. | en |
dc.language.iso | en | en |
dc.subject | DRNTU::Science::Chemistry::Biochemistry | en |
dc.title | Mutagenesis studies to determine the key interfacial amino acid residues that govern the self-assembly of the ferritin protein cages | en |
dc.type | Thesis | en |
dc.contributor.supervisor | Brendan Patrick Orner | en |
dc.contributor.school | School of Physical and Mathematical Sciences | en |
dc.description.degree | DOCTOR OF PHILOSOPHY (SPMS) | en |
dc.identifier.doi | 10.32657/10356/48015 | en |
item.fulltext | With Fulltext | - |
item.grantfulltext | open | - |
Appears in Collections: | SPMS Theses |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Tspms0702534E_Zhang+Yu's+thesis.pdf | main article | 82.45 MB | Adobe PDF | View/Open |
Page view(s) 50
596
Updated on Mar 27, 2024
Download(s) 20
272
Updated on Mar 27, 2024
Google ScholarTM
Check
Altmetric
Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.