Bethesda, MD - The November 1st and November 15th issues of Biophysical Journal, published by the Biophysical Society, are now available online. Topics of interest include voltage-gated potassium channels that could payoff in synthetic drug design, the absence of large lipid rafts in cells, and the structure of a Na+/H+ antiporter dimmer.
Volume 93, Issue 9, November 1, 2007
Dynamics of the Kv1.2 voltage-gated K+ channel in a Membrane Environment
Vishwanath Jogini, University of Chicago and Benoit Roux, University of Chicago
Keywords: arginine; electrostatics; free energy; membrane voltage; phospholipid; salvation
Using powerful computers at Argonne National Laboratory, scientists have taken a step closer to understanding how voltage-gated potassium channels work. Vishwanath Jogini and Benot Roux, researchers in the University of Chicagos Institute of Molecular Pediatric Science, used the large-scale computers in Argonnes Laboratory Computing Resource Center to conduct simulations of the channels in mammalian cells.
The features revealed by these computer simulations could lead to medical breakthroughs in synthetic drug design.
Specifically, Jogini and Roux produced molecular dynamic simulations of a detailed atomic model of the Kv1.2 voltage-gated potassium channel in an explicit membrane using the crystallographic x-ray structure determined by Rod MacKinnon (Rockefeller University) and his collaborators in 2005.
A long-term endeavor of biophysical research is to advance our understanding of these proteins and predict their function. The voltage-gated channels regulate the generation and spread of electrical signals in neurons, muscles, and other excitable cells. These minuscule electrical signals carry nerve impulses and control muscle contractions.
In humans, malfunction of these channels can result in neurological or cardiovascular diseases, such as cardiac arrh
|Contact: Ellen R. Weiss|