Frankel:Force Spectroscopy: Difference between revisions

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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>Nano-mechanics of HIV GP160</font>'''




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'''<font color=#000000 font size=3 font align="justify">  
'''<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.
Typical sawtooth unfolding pattern of a single molecule of the HIV virion protein GP160. Unfolding forces can be extracted from the sawtooth pattern by applying the worm like chain model.</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>'''




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'''<font color=#000000 font size=3> Revealing the selective interactions of fibronectin with lipid bilayer. </font>'''
'''<font color=#000000 font size=3> Unfolding the ECM protein fibronectin </font>'''




Revision as of 14:44, 7 January 2013

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'______ 'Force Spectroscopy


HIV-gp160

Assembly

Nano-mechanics of HIV GP160


GP160mica

Typical sawtooth unfolding pattern of a single molecule of the HIV virion protein GP160. Unfolding forces can be extracted from the sawtooth pattern by applying the worm like chain model.





Unfolding the ECM protein fibronectin




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.

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