Biomod/2011/Tianjin:Results: Difference between revisions

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=Results=
=Results=
==A==
==1==
[[Image:Biomod tianjin results 1.png|center|650px|thumb|Fig 1 ]]
[[Image:Biomod tianjin results 1.png|center|650px|thumb|Fig 1.AFM analysis of MreB-RFP cell-free aggregation with SWNTs, indicating that SWNTs serve as scaffolds in the spiral winding of fusion proteins in vitro.
*a). AFM image of fusion protein MreB-RFP without SWNT scaffold, protein aggregated in disorder and only discrete spherical particles were formed.
*b). AFM image of fusion protein MreB-RFP at the presence of SWNT, protein aggregated
and wound spirally onto the surface of nanotube.
]]


==A==
==2==
[[Image:Biomod tianjin results 24.png|center|650px|thumb|Fig 2 ]]
[[Image:Biomod tianjin results 24.png|center|650px|thumb|Fig 2. SEM analysis of MreB-RFP cell-free aggregation with SWNTs.
*a). SEM image of SWNT, the sidewall of nanotube is smooth
without any absorption or aggregation.
*b). SEM image of MreB-RFP without scaffold, protein aggregated
in disorder and only discrete spherical particles were formed.
*c). SEM image of fusion protein at the presence of SWNT, protein
aggregated and wound spirally onto the surface of nanotube.
]]


==A==
==3==
[[Image:Biomod tianjin results 3.png|center|650px|thumb|Fig 3 ]]
[[Image:Biomod tianjin results 3.png|center|650px|thumb|Fig 3. TEM analysis of MreB-RFP cell-free aggregation with SWNTs.
*a). TEM image of SWNT, the sidewall of nanotube is smooth
without any absorption or aggregation.
*b). TEM image of MreB-RFP without scaffold, protein aggregated
in disorder and only discrete spherical particles were formed.
*c). TEM image of fusion protein without SWNT scaffold, protein
aggregated and wound spirally onto the surface of SWNT.
]]


==A==
==4==
[[Image:Biomod tianjin results 4.png|center|500px|thumb|Fig 4 ]]
[[Image:Biomod tianjin results 4.png|center|500px|thumb|Fig 4. Fluorescence micrograph of fusion protein MreB combined with SWNT. Red fluorescence can be observed, indicating the activity of fusion protein were reserved. ]]




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Revision as of 11:57, 31 October 2011


Home            Project            Results            Video            Team            Acknowledgements

Results

1

Fig 1.AFM analysis of MreB-RFP cell-free aggregation with SWNTs, indicating that SWNTs serve as scaffolds in the spiral winding of fusion proteins in vitro. *a). AFM image of fusion protein MreB-RFP without SWNT scaffold, protein aggregated in disorder and only discrete spherical particles were formed. *b). AFM image of fusion protein MreB-RFP at the presence of SWNT, protein aggregated and wound spirally onto the surface of nanotube.

2

Fig 2. SEM analysis of MreB-RFP cell-free aggregation with SWNTs. *a). SEM image of SWNT, the sidewall of nanotube is smooth without any absorption or aggregation. *b). SEM image of MreB-RFP without scaffold, protein aggregated in disorder and only discrete spherical particles were formed. *c). SEM image of fusion protein at the presence of SWNT, protein aggregated and wound spirally onto the surface of nanotube.

3

Fig 3. TEM analysis of MreB-RFP cell-free aggregation with SWNTs. *a). TEM image of SWNT, the sidewall of nanotube is smooth without any absorption or aggregation. *b). TEM image of MreB-RFP without scaffold, protein aggregated in disorder and only discrete spherical particles were formed. *c). TEM image of fusion protein without SWNT scaffold, protein aggregated and wound spirally onto the surface of SWNT.

4

Fig 4. Fluorescence micrograph of fusion protein MreB combined with SWNT. Red fluorescence can be observed, indicating the activity of fusion protein were reserved.


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