Difference between revisions of "Frankel:Cyberplasm"

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''< font color=#ffffff font size=8>_________ </font>'''''<font color=#000000 font size=6> Cyberplasm - a biohybrid swimming robot</font>'''
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''<font align="center" font color=#ffffff font size=8>_________ </font>'''''<font color=#000000 font size=6>Biohybrid Machines </font>'''
 
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''<font align="center" font color=#ffffff font size=8>_______ </font>'''''<font color=#000000 font size=3>Cyberplasm</font>'''
  
[[Image:HIV1.png|500px]]
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[[Image:Cyberplasm.png|500px]]
  
 
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[[Image:FNselec.png|235px]]
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[[Image:GP160_on_mica.png|235px]]
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[[Image:FNseleczoom.png|235px]]
[[Image:GP160_on_DOPC.png|235px]]
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[[Image:Pore50nm.png|235px]]
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[[Image:Pore100nm.png|235px]]
 
[[Image:GP160.png|235px]]
 
  
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[[Image:FN_complexes.jpg|235px]]
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[[Image:FN_adsorbed.jpg|235px]]
 
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'''<font color=#000000 font size=3>HIV covers its protein capsid with a viral envelop where GP160 is located. This glycoprotein 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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[[Image:FNint.png|500px]]
 
 
[[Image:GIF-VIRUS-INFECTION1.gif|500px]]
 
 
   
 
   
  
 
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'''<font color=#000000 font size=3> One of the major components of the extracellular matrix (ECM) is fibronectin, this dimeric glycoprotein is involved in numerous cell processes and has important functions in vertebrate development.  
  
'''<font color=#000000 font size=3>The images to the right show the self assembly of the HIV gp160 protein reconstituted into DOPC bilayer and adsorbed onto mica. Each pore is made up of 6 features with dimensions consistent with single molecules</font>'''
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Fibronectin in the extracellular matrix interacts with the transmembrane integrins in a highly specific manner. The ECM ligand protein contains a tripeptide recognition site, Arg-Gly-Asp (RGD), responsible for the affinity of the cell surface receptors with its ligand.
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Atomic force microscopy images can be appreciated, these illustrations depict how fibronectin molecules are almost exclusively absorbed on the DPPC domains.

Latest revision as of 10:16, 2 March 2013

<owwmenu align="center" font="helvetica" bold="1" color="white" bgcolor="black" hovercolor="black" bghovercolor="orange" topfontsize="10" fontSize="10" image="Danbanner-bio-machines.jpg" >

Home=Frankel Members=#,Principal Investigator=Frankel:Lab_Members, PhD students=Frankel:Lab_Members, Alumni=Frankel:Lab_Members Contact=Frankel:Contact Collaborators=Frankel:Collaborators Publications=Frankel:Publications Lab=Frankel:Research Research=#,Force Spectroscopy=Frankel:Force Spectroscopy,HIV/Virus=Frankel:HIV/Virus,ECM Proteins=Frankel:ECM Proteins,Cyberplasm=Frankel:Cyberplasm,Cancer=Frankel:Cancer

_________ Biohybrid Machines



FNselec.png

FNseleczoom.png

FN complexes.jpg

FN adsorbed.jpg





FNint.png



One of the major components of the extracellular matrix (ECM) is fibronectin, this dimeric glycoprotein is involved in numerous cell processes and has important functions in vertebrate development.

Fibronectin in the extracellular matrix interacts with the transmembrane integrins in a highly specific manner. The ECM ligand protein contains a tripeptide recognition site, Arg-Gly-Asp (RGD), responsible for the affinity of the cell surface receptors with its ligand. Atomic force microscopy images can be appreciated, these illustrations depict how fibronectin molecules are almost exclusively absorbed on the DPPC domains.