Study on the Self-assembly of Bacterial Crystalline Surface Protein by Using Coulter Multisizer
| Autor: | yi-bin Liu, 劉以斌 |
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| Rok vydání: | 2003 |
| Druh dokumentu: | 學位論文 ; thesis |
| Popis: | 91 The S-layer of Deinococcus radiodurans IR is a two-dimensional crystalline array on the cell surface composed of a single protein, (S-layer protein, SLP). We have established conditions for preparation of stable, soluble and then efficient in vitro self-assembly of the purify protein. The self-assembly products (SAs) obtain through addition-removal protocol of hydrogen-bond breaking agent (guanidine hydrochloride). SAs are lamella and micrometer scale structure in average diameter by light microscopy observation. SAs also represent paracrystalline regular array structure by transmission electron microscopy observation (25~50 nm per unit diameter). Furthermore, we have successful monitored the variation of SAs particlenumber and size distribution (＞0.2 μm3) in self-assembly process. We also research the thermal effect of SAs self-assembly process. We have demonstrated the SAs are highly thermal resistant and found periodicity in SAs self-assembly process. These results reveal that the self-assembly is time and temperature dependent. COULTER size analysis could be potential tool for study the self-assembly mechanism in the bio- and nanotechnology. |
| Databáze: | Networked Digital Library of Theses & Dissertations |
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