Bilayers A Structural Mechanism for MscS Gating in Lipid
نویسنده
چکیده
www.sciencemag.org (this information is current as of October 17, 2008 ): The following resources related to this article are available online at http://www.sciencemag.org/cgi/content/full/321/5893/1210 version of this article at: including high-resolution figures, can be found in the online Updated information and services, http://www.sciencemag.org/cgi/content/full/321/5893/1210/DC1 can be found at: Supporting Online Material found at: can be related to this article A list of selected additional articles on the Science Web sites http://www.sciencemag.org/cgi/content/full/321/5893/1210#related-content http://www.sciencemag.org/cgi/content/full/321/5893/1210#otherarticles , 20 of which can be accessed for free: cites 39 articles This article http://www.sciencemag.org/cgi/collection/biochem Biochemistry : subject collections This article appears in the following http://www.sciencemag.org/about/permissions.dtl in whole or in part can be found at: this article permission to reproduce of this article or about obtaining reprints Information about obtaining
منابع مشابه
Molecular Insight into the Mutual Interactions of Two Transmembrane Domains of Human Glycine Receptor (TM23-GlyR), with the Lipid Bilayers
Appearing as a computational microscope, MD simulation can ‘zoom in’ to atomic resolution to assess detailed interactions of a membrane protein with its surrounding lipids, which play important roles in the stability and function of such proteins. This study has employed the molecular dynamics (MD) simulations, to determine the effect of added DMPC or DMTAP molecules on the structure of D...
متن کاملMagic Angle Spinning Nuclear Magnetic Resonance Characterization of Voltage-Dependent Anion Channel Gating in Two-Dimensional Lipid Crystalline Bilayers
The N-terminus of the voltage-dependent anion channel (VDAC) has been proposed to contain the mechanistically important gating helices that modulate channel opening and closing. In this study, we utilize magic angle spinning nuclear magnetic resonance (MAS NMR) to determine the location and structure of the N-terminus for functional channels in lipid bilayers by measuring long-range (13)C-(13)C...
متن کاملاثرات میدان الکترومغناطیسی تلفن همراه بر عملکرد تک نانوکانال پروتیینی OmpF: یک رویکرد تجربی
Background: Widespread of telecommunication systems in recent years, have raised the concerns on the possible danger of cell phone radiations on human body. Thus, the study of the electromagnetic fields on proteins, particularly the membrane nano channel forming proteins is of great importance. These proteins are responsible for keeping certain physic-chemical condition within cells and managin...
متن کاملProbing the structure of the mechanosensitive channel of small conductance in lipid bilayers with pulsed electron-electron double resonance.
Mechanosensitive channel proteins are important safety valves against osmotic shock in bacteria, and are involved in sensing touch and sound waves in higher organisms. The mechanosensitive channel of small conductance (MscS) has been extensively studied. Pulsed electron-electron double resonance (PELDOR or DEER) of detergent-solubilized protein confirms that as seen in the crystal structure, th...
متن کاملStructural dynamics of the S4 voltage-sensor helix in lipid bilayers lacking phosphate groups.
Voltage-dependent K(+) (Kv) channels require lipid phosphates for functioning. The S4 helix, which carries the gating charges in the voltage-sensing domain (VSD), inserts into membranes while being stabilized by a protein-lipid interface in which lipid phosphates play an essential role. To examine the physical basis of the protein-lipid interface in the absence of lipid phosphates, we performed...
متن کاملGlobal structural changes of an ion channel during its gating are followed by ion mobility mass spectrometry.
Mechanosensitive ion channels are sensors probing membrane tension in all species; despite their importance and vital role in many cell functions, their gating mechanism remains to be elucidated. Here, we determined the conditions for releasing intact mechanosensitive channel of large conductance (MscL) proteins from their detergents in the gas phase using native ion mobility-mass spectrometry ...
متن کامل