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made with VMD
The 2.12 release of the molecular dynamics program NAMD provides major enhancements in performance, flexibility, and accuracy, complementing the greatly enhanced usability provided by the QwikMD GUI released in VMD 1.9.3. NVIDIA GPU-accelerated simulations with NAMD 2.12 are up to three times as fast as 2.11, particularly for implicit solvent simulations and single-node simulations of smaller systems. NAMD 2.12 is also optimized for the new Intel Xeon Phi KNL processors found in Argonne Theta, NERSC Cori, and TACC Stampede 2. NAMD 2.12 builds on the asynchronous multi-copy scripting capabilities introduced in NAMD 2.11 with the ability to modify and reload the molecular structure, enabling development of grand canonical and constant pH ensemble methods, as well as an optional Python interface for advanced on-the-fly analysis. Finally, NAMD 2.12 provides a complete, no-recompilation-needed interface for hybrid QM/MM with both the semi-empirical code MOPAC and the ab initio/DFT code ORCA. More on new features in the 2.12 release of NAMD can be found here. NAMD is available free-of-charge as source code, precompiled binaries, pre-installed at supercomputer centers, and now jointly with VMD as one-click interactive molecular modeling on the Amazon cloud.
made with VMD
The latest release of VMD brings many advances that help researchers prepare, analyze, and visualize molecular simulations. The new QwikMD plugin streamlines key simulation preparation and analysis tasks, and guides users in the creation of reusable simulation workflows and protocols. VMD now includes several advanced features for parallel analysis and visualization of cellular-scale simulations, as reported here, and here. VMD 1.9.3 strengthens collaboration between experimental and computational biologists by supporting a broader range of experimental density map image formats, such as those used in cryo-electron tomography. Many updated plugins are included in VMD 1.9.3, including tools for analysis of free energy perturbation simulations, MDFF hybrid structure fitting, ffTK force field parameterization, and normal mode analysis. VMD 1.9.3 adds support for new hardware and operating system platforms including IBM OpenPOWER (ORNL Summit), a variety of GPU-accelerated ARM SoCs, the Amazon AWS EC2 cloud, and most recently, the Intel Xeon Phi Knight's Landing many-core CPU (TACC Stampede 2, Argonne Theta). The VMD 1.9.3 release adds stunning graphics produced using interactive ray tracing using the latest multi-core CPUs and GPU accelerators, enabling 360-degree panoramic movie rendering for VR headsets, as reported here, and here. Interactive ray tracing makes the task of getting a molecular image "just right" much easier than ever before; it also enables rendering of spectacular movies for communication of scientific results. A VR movie rendering tutorial assists users with the steps required in rendering and encoding VR movies for upload to YouTube for display using VR headsets such as Google Cardboard, Oculus Rift, and GearVR. More details about VMD 1.9.3 features can be found here.
made with VMD
ATP, a ubiquitously prevalent biomolecule, which is best known for being the principal energy source for a living cell, also plays a crucial role in inter-cellular communication, thus acting as a signaling molecule. One of the major receptors in this signaling cascade are the P2X receptors which are trimeric, non-selective cation channel activated by ATP and responsible for key processes such as muscle contraction, inflammatory response, pain, and even taste signal transduction. As a result of their extensive prevalence and important implications in human physiology, P2X receptors serve as important pharmacological targets for cardiovascular, neuronal, and inflammatory diseases. In a recent collaborative study with experimental structural biologists, molecular dynamics simulations of a membrane-embedded model of a P2X receptor performed with NAMD were used to reveal intricate details of the ion permeation mechanism and pathway. Surprisingly, it was observed that one half of the ion permeation pathway is composed of lipids on one side and of the protein residues on the other side, a novel design for an ion translocation pore. The study demonstrates yet another active functional role for lipids in membrane protein function, further emphasizing the importance of lipid protein interactions in biological processes. More details can be found here.