1c:{"metadata":[["$","title","0",{"children":"NIH VideoCast - Zinc-Finger Protein HIV-1 Nucleocapsid p7 Studied by Electron Capture Dissociation ESI-FTMS"}],["$","meta","1",{"name":"description","content":" HIV-1 nucleocapsid protein p7 (NC) is a \nzinc-finger protein that plays\n crucial roles in genome recognition, dimerization, and \npackaging of viral RNA into\n infectious particles. Much of the functionality of NC is \nbelieved to arise from the specific\n architecture of its two zinc-finger domains, which are \nhighly conserved regions found in\n all known retroviruses. Prior studies have shown that \nmutation of NC zinc-finger\n domains renders the viral particle non-infectious. \nTherefore, complete elucidation of the\n chaperone properties and RNA-binding mechanism of NC are \nnecessary for the\n development of small drug inhibitors aimed at disrupting \nthe packaging of the AIDS\n virus.\n\n

\nFor more information, visit the Mass Spectrometry Interest Group of the NCI at Frederick
"}],["$","meta","2",{"name":"publisher","content":"National Institutes of Health"}],["$","meta","3",{"property":"og:title","content":"NIH VideoCast - Zinc-Finger Protein HIV-1 Nucleocapsid p7 Studied by Electron Capture Dissociation ESI-FTMS"}],["$","meta","4",{"property":"og:description","content":" HIV-1 nucleocapsid protein p7 (NC) is a \nzinc-finger protein that plays\n crucial roles in genome recognition, dimerization, and \npackaging of viral RNA into\n infectious particles. Much of the functionality of NC is \nbelieved to arise from the specific\n architecture of its two zinc-finger domains, which are \nhighly conserved regions found in\n all known retroviruses. Prior studies have shown that \nmutation of NC zinc-finger\n domains renders the viral particle non-infectious. \nTherefore, complete elucidation of the\n chaperone properties and RNA-binding mechanism of NC are \nnecessary for the\n development of small drug inhibitors aimed at disrupting \nthe packaging of the AIDS\n virus.\n\n

\nFor more information, visit the Mass Spectrometry Interest Group of the NCI at Frederick
"}],["$","meta","5",{"property":"og:url","content":"https://uat.d1rkikwu4q8tg.amplifyapp.com/watch/97b682e6-d5db-11f0-9cf9-12c45c580ad9"}],["$","meta","6",{"property":"og:site_name","content":"NIH VideoCast"}],["$","meta","7",{"property":"og:image","content":"https://nihcit.rev.vbrick.com/api/v2/media/videos/thumbnails/7b978198-8cd5-4eb5-999d-cde39a24d600.jpg"}],["$","meta","8",{"property":"og:type","content":"website"}],["$","meta","9",{"name":"twitter:card","content":"summary_large_image"}],["$","meta","10",{"name":"twitter:title","content":"NIH VideoCast - Zinc-Finger Protein HIV-1 Nucleocapsid p7 Studied by Electron Capture Dissociation ESI-FTMS"}],["$","meta","11",{"name":"twitter:description","content":" HIV-1 nucleocapsid protein p7 (NC) is a \nzinc-finger protein that plays\n crucial roles in genome recognition, dimerization, and \npackaging of viral RNA into\n infectious particles. Much of the functionality of NC is \nbelieved to arise from the specific\n architecture of its two zinc-finger domains, which are \nhighly conserved regions found in\n all known retroviruses. Prior studies have shown that \nmutation of NC zinc-finger\n domains renders the viral particle non-infectious. \nTherefore, complete elucidation of the\n chaperone properties and RNA-binding mechanism of NC are \nnecessary for the\n development of small drug inhibitors aimed at disrupting \nthe packaging of the AIDS\n virus.\n\n

\nFor more information, visit the Mass Spectrometry Interest Group of the NCI at Frederick
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