NIH VideoCast - Membranes, the Flu and in Between

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Membranes, the Flu and in Between

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Air date:	Tuesday, August 11, 2009, 11:00:00 AM Time displayed is Eastern Time, Washington DC Local
Views:	Total views: 125 * This only includes stats from October 2011 and forward.
Category:	Special
Runtime:	00:59:15
Closed captioning:	Check box to display CC outside of the video Note: You can drag the captioning window around and resize it
Description:	After receiving his Ph.D. from Yale University with Don Engelman and Steve Smith in 1995, Dr. Arkin remained for one year at Yale for postdoctoral training with Axel Brunger. From 1997-2000, Dr. Arkin worked as a Lecturer at the University of Cambridge (UK) before becoming an Associate Professor at the Hebrew University of Jerusalem. He was a visiting scientist at DE Saw Research from 2005-2006, and was promoted to Full Professor at the Hebrew University in 2005. Since 2008, he has been Head of the Life Sciences Institute at the Hebrew University. Dr. Arkin’s seminar entitled ‘Membranes, the flu and in between’ will cover the following three interrelated topics: The fundamental reason why transmembrane helices are so hydrophobic. Here we show that the reason for their extreme hydrophobicity is not the physical constraints of the lipid bilayer but rather the specificity of the secretion apparatus. How the influenza M2 H+ channel is gated. Here we have unraveled the rotation-based gating of the channel using unbiased restraints from linear and 2D IR spectroscopy. We also present a simple approach to identify new blockers against the channel. Mechanism of cation specificity of Na+/H+ antiporters. Surprisingly, computational analysis has showed that the Na+ specificity of the pump over K+ does not take place at the binding stage. Experimental data corroborate this conclusion, providing new insight into the how the protein can discriminate between two very similar cations. The SBIG is a clearinghouse for discussions and interactions between scientists interested in all aspects of molecular structure, from experimental determination by x-ray crystallography, electron microscopy, mass spectrometry, and NMR, to theoretical and computational biology and biophysics, and to the biological application of structural data. For more information, visit Structural Biology Interest Group

NLM Title:	Membranes, the flu and in between / Isaiah Arkin.
Author:	Arkin, Isaiah. National Institutes of Health (U.S.). Structural Biology Interest Group.
Publisher:
Abstract:	(CIT): After receiving his Ph.D. from Yale University with Don Engelman and Steve Smith in 1995, Dr. Arkin remained for one year at Yale for postdoctoral training with Axel Brunger. From 1997-2000, Dr. Arkin worked as a Lecturer at the University of Cambridge (UK) before becoming an Associate Professor at the Hebrew University of Jerusalem. He was a visiting scientist at DE Saw Research from 2005-2006, and was promoted to Full Professor at the Hebrew University in 2005. Since 2008, he has been Head of the Life Sciences Institute at the Hebrew University. Dr. Arkin"s seminar entitled "Membranes, the flu and in between" will cover the following three interrelated topics: The fundamental reason why transmembrane helices are so hydrophobic. Here we show that the reason for their extreme hydrophobicity is not the physical constraints of the lipid bilayer but rather the specificity of the secretion apparatus. How the influenza M2 H+ channel is gated. Here we have unraveled the rotation-based gating of the channel using unbiased restraints from linear and 2D IR spectroscopy. We also present a simple approach to identify new blockers against the channel. Mechanism of cation specificity of Na+/H+ antiporters. Surprisingly, computational analysis has showed that the Na+ specificity of the pump over K+ does not take place at the binding stage. Experimental data corroborate this conclusion, providing new insight into the how the protein can discriminate between two very similar cations. The SBIG is a clearinghouse for discussions and interactions between scientists interested in all aspects of molecular structure, from experimental determination by x-ray crystallography, electron microscopy, mass spectrometry, and NMR, to theoretical and computational biology and biophysics, and to the biological application of structural data. For more information, visit Structural Biology Interest Group.
Subjects:	Hydrophobic and Hydrophilic Interactions Ion Channels--physiology Membrane Potentials--physiology Protein Transport--physiology
Publication Types:	Lecture Webcast
NLM Classification:	QU 55.7
NLM ID:	101514417
CIT Live ID:	7832
Permanent link:	https://videocast.nih.gov/watch=7832

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