Difference between revisions of "Frankel:Force Spectroscopy"

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'''<font color=#FFFFFF font size=3>Assembly</font>'''
 
'''<font color=#FFFFFF font size=3>Assembly</font>'''
  
 
'''<font color=#000000 font size=3>Self assembly and pore formation of HIV GP160 revealed at molecular resolution</font>'''
 
'''<font color=#000000 font size=3>Self assembly and pore formation of HIV GP160 revealed at molecular resolution</font>'''
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[[Image:GP160mica.png|300px]]
 
[[Image:GP160mica.png|300px]]
  
'''<font color=#FFFFFF font size=3>GP160mica</font>'''
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'''<font color=#FFFFFF font size=6>GP160mica</font>'''
  
 
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'''<font color=#000000 font size=3 font align="justify">  
 
Force spectra taken on raised terraces and lower features. Rupture force distribution of self assembled gp160 unfolding on terraced and lower regions.
 
Force spectra taken on raised terraces and lower features. Rupture force distribution of self assembled gp160 unfolding on terraced and lower regions.
 
Rupture forces were measured as 79.6 ± 3.9 pN and 81.3 ± 3.8 pN for the terraces and lower regions, respectively. These forces are much lower than those measured for unfolding of isolated proteins on mica, which were above 160 pN. The lower unfolding forces suggest that GP160 is considerably easier to unfold when aggregated than isolated.</font>'''
 
Rupture forces were measured as 79.6 ± 3.9 pN and 81.3 ± 3.8 pN for the terraces and lower regions, respectively. These forces are much lower than those measured for unfolding of isolated proteins on mica, which were above 160 pN. The lower unfolding forces suggest that GP160 is considerably easier to unfold when aggregated than isolated.</font>'''

Revision as of 12:11, 9 November 2012

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Force Spectroscopy


Assembly

Self assembly and pore formation of HIV GP160 revealed at molecular resolution


GP160mica.png

GP160mica

Stlow.png Hislow.png Sttr.png Histr.png


Force spectra taken on raised terraces and lower features. Rupture force distribution of self assembled gp160 unfolding on terraced and lower regions. Rupture forces were measured as 79.6 ± 3.9 pN and 81.3 ± 3.8 pN for the terraces and lower regions, respectively. These forces are much lower than those measured for unfolding of isolated proteins on mica, which were above 160 pN. The lower unfolding forces suggest that GP160 is considerably easier to unfold when aggregated than isolated.





Revealing the selective interactions of fibronectin with lipid bilayer.


FNsawt.png


HisFN.png



Sawtooth pattern on the retraction force curve indicating the unfolding of fibronectin. The average rupture force distribution of the protein on mica surface was 85.1 ± 2.7 pN.