Frankel:HIV/Virus

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'''<font color=#045FB4 font size=3>SELF ASSEMBLY AND PORE FORMATION OF HIV GP160 REVEALED AT MOLECULAR RESOLUTION </font>'''
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'''<font color=#045FB4 font size=3>HIV covers its protein capsid with a viral envelop where a glycoprotein (GP160) is located. This protein facilitates fusion between the viral membrane and the host -cell membrane allowing liberation of the viral contents into the host cell. GP160 forms a trimer, where each monomer consists in two non-covalently associated subunits: a surface subunit GP120 that recognize and bind to specific receptor on the host cell and a transmembrane subunit GP41 that promotes membrane fusion.</font>'''
   
   
   
   
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'''<font color=#045FB4 font size=3>ATOMIC FORCE MICROSCOPY IMAGES SELF ASSEMBLY OF HIV GP160 RECONSTITUTED INTO DOPC BILAYER AND ADSORBED ONTO MICA. GP160 FORMING PORE.LIKE  TRUCTURES </font>'''
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'''<font color=#045FB4 font size=3> Self assembly and pore formation of HIV gp160 revealed at molecular resolution
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Self assembly of HIV gp160 reconstituted into DOPC bilayer and adsorbed onto mica.
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gp160 forming pore like structures. </font>'''

Revision as of 20:55, 8 November 2012

Danbanner-bio-machines.jpg


HIV gp160







HIV covers its protein capsid with a viral envelop where a glycoprotein (GP160) is located. This protein facilitates fusion between the viral membrane and the host -cell membrane allowing liberation of the viral contents into the host cell. GP160 forms a trimer, where each monomer consists in two non-covalently associated subunits: a surface subunit GP120 that recognize and bind to specific receptor on the host cell and a transmembrane subunit GP41 that promotes membrane fusion.



Self assembly and pore formation of HIV gp160 revealed at molecular resolution

Self assembly of HIV gp160 reconstituted into DOPC bilayer and adsorbed onto mica.

gp160 forming pore like structures.