Zinc-Finger Protein HIV-1 Nucleocapsid p7 Studied by Electron Capture Dissociation ESI-FTMS

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Air date:	Tuesday, November 18, 2003, 2:00:00 PM Time displayed is Eastern Time, Washington DC Local
Views:	Total views: 116 * This only includes stats from October 2011 and forward.
Category:	Special
Runtime:	00:37:04
Closed captioning:	Check box to display CC outside of the video Note: You can drag the captioning window around and resize it
Description:	HIV-1 nucleocapsid protein p7 (NC) is a zinc-finger protein that plays crucial roles in genome recognition, dimerization, and packaging of viral RNA into infectious particles. Much of the functionality of NC is believed to arise from the specific architecture of its two zinc-finger domains, which are highly conserved regions found in all known retroviruses. Prior studies have shown that mutation of NC zinc-finger domains renders the viral particle non-infectious. Therefore, complete elucidation of the chaperone properties and RNA-binding mechanism of NC are necessary for the development of small drug inhibitors aimed at disrupting the packaging of the AIDS virus. For more information, visit the Mass Spectrometry Interest Group of the NCI at Frederick

NLM Title:	Zinc-finger protein HIV-1 nucleocapsid p7 studied by electron capture dissociation ESI-FTMS / Katherine Kellersberger.
Author:	Kellersberger, Katherine. National Institutes of Health (U.S.)
Publisher:
Subjects:	Capsid Proteins Gene Products, gag HIV-1 Spectrometry, Mass, Electrospray Ionization
Publication Types:	Lecture Webcast
Rights:	This is a work of the United States Government. No copyright exists on this material. It may be disseminated freely.
NLM Classification:	QW 168.5.H6
NLM ID:	101268292
CIT Live ID:	2929
Permanent link:	https://videocast.nih.gov/watch=2929

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