Reconfiguration of the proteasome during chaperone-mediated assembly. Park S, Li X et al. Nature. 2013 May 23;497:512–6.
Rational HIV immunogen design to target specific germline B cell receptors. Jardine J, Julien JP et al. Science. 2013 May 10;340(6133):711-6.
Self-assembling cages from coiled-coil peptide modules. Fletcher JM, Harniman RL et al. Science. 2013 May 3;340(6132):595-9.
A conformational switch in HP1 releases auto-inhibition to drive heterochromatin assembly. Canzio D, Liao M et al. Nature. 2013 Apr 18;496(7445):377-81.
The bacterial DnaC helicase loader is a DnaB ring breaker. Arias-Palomo E, O'Shea VL et al. Cell. 2013 Apr 11;153(2):438-48.(Previously featured citations...)
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April 18, 2013
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A production release candidate (version 1.7) is now available; please try it and report any problems. See the release notes for changes relative to the previous release. Mac PowerPC and OS X 10.5 are no longer supported.(Previous news...)
UCSF Chimera is a highly extensible program for interactive visualization and analysis of molecular structures and related data, including density maps, supramolecular assemblies, sequence alignments, docking results, trajectories, and conformational ensembles. High-quality images and animations can be generated. Chimera includes complete documentation and several tutorials, and can be downloaded free of charge for academic, government, non-profit, and personal use. Chimera is developed by the Resource for Biocomputing, Visualization, and Informatics, funded by the National Institutes of Health (NIGMS P41-GM103311).
There are several ways to superimpose structures in Chimera:
• MatchMaker performs a fit after automatically identifying which residues should be paired. Pairing uses both sequence and secondary structure, allowing similar structures to be superimposed even when their sequence similarity is low to undetectable.
The figure shows five distantly related proteins (pairwise sequence identities <25%) from the SCOP WD40 superfamily before and after MatchMaker superposition with default parameters.
• Structures can be matched using a pre-existing sequence alignment.
• The exact atoms to pair can be specified with the match command. This works on any type of structure, while the preceding methods apply only to peptide and nucleotide chains.
• Structures can be superimposed manually by activating/deactivating them for motion and using the mouse.
Potassium channel (Protein Data Bank entry 1bl8) on a dark slate blue background with potassium ions shown in firebrick. The channel is comprised of four chains. Each chain has been rainbow-colored from blue at the N-terminus to red at the C-terminus, but only the surface of the channel is shown. The surface has been sliced with a per-model clipping plane. The surface cap color is plum except with opacity set to 0.8. The shininess and brightness have been set to 128 and 8, respectively, and the lights on the scene have been moved from their default positions. The subdivision quality (related to the smoothness of the spherical ions) is 5.0, and the molecular surface was computed with probe radius and vertex density set to 1.0 and 6.0, respectively. (More samples...)