Denaturants effect on E2 protein
The self-assembly of a protein cage composed of the catalytic core domain of pyruvate dehydrogenase multienzyme complex (E2) was investigated. E2 was produced in Escherichia coli (BL21 (DE3)). The hydrodynamic size of E2 was measured to be 27-28 nm using Dynamic Light Scattering technique. E2 was su...
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| Format: | Final Year Project |
| Language: | English |
| Published: |
2009
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| Online Access: | http://hdl.handle.net/10356/16871 |
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| Institution: | Nanyang Technological University |
| Language: | English |
| Summary: | The self-assembly of a protein cage composed of the catalytic core domain of pyruvate dehydrogenase multienzyme complex (E2) was investigated. E2 was produced in Escherichia coli (BL21 (DE3)). The hydrodynamic size of E2 was measured to be 27-28 nm using Dynamic Light Scattering technique. E2 was subjected to various concentrations of two denaturants, urea and guanidine hydrochloride (GuHCl). The observed size of E2 started to decrease in the presence of 2.5 M GuHCl and drastically degrade up to half of its initial size in the presence of 3.5 M GuHCl. There was no significant change in the size of E2 protein upon incubation with various concentration of urea for one hour. |
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