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The structure of apolipoprotein B100 from human low-density lipoprotein. Berndsen ZT, Cassidy CK. Nature. 2025 Feb 20;638(8051):836–843.
Bat genomes illuminate adaptations to viral tolerance and disease resistance. Morales AE, Dong Y et al. Nature. 2025 Feb 13;638(8050):449–458.
C-terminal amides mark proteins for degradation via SCF-FBXO31. Muhar MF, Farnung J et al. Nature. 2025 Feb 13;638(8050):519–527.
Resolving native GABAA receptor structures from the human brain. Zhou J, Noviello CM et al. Nature. 2025 Feb 13;638(8050):562–568.
Four-component protein nanocages designed by programmed symmetry breaking. Lee S, Kibler RD et al. Nature. 2025 Feb 13;638(8050):546–552.
More citations...News
December 25, 2024
|
December 12, 2024
The ChimeraX 1.9 production release is available! See the change log for what's new.
October 14, 2024
Planned downtime: The ChimeraX website, Toolshed, web services (Blast Protein, Modeller, ...) and cgl.ucsf.edu e-mail will be unavailable starting Monday, Oct 14 10 AM PDT, continuing throughout the week and potentially the weekend (Oct 14-20).
Previous news...Upcoming Events
UCSF ChimeraX (or simply ChimeraX) is the next-generation molecular visualization program from the Resource for Biocomputing, Visualization, and Informatics (RBVI), following UCSF Chimera. ChimeraX can be downloaded free of charge for academic, government, nonprofit, and personal use. Commercial users, please see ChimeraX commercial licensing.
ChimeraX is developed with support from National Institutes of Health R01-GM129325, Chan Zuckerberg Initiative grant EOSS4-0000000439, and the Office of Cyber Infrastructure and Computational Biology, National Institute of Allergy and Infectious Diseases.
Feature Highlight
Molecular lipophilicity potential (MLP) can be calculated for a protein
and displayed with surface coloring using the command
mlp or the
Molecule Display
icon
.
The image shows the photosynthetic reaction center from a
purple sulfur bacterium, with MLP coloring on the molecular surface
and membrane boundaries from OPM (Orientations of Proteins in Membranes
entry 1eys).
Blue and red balls represent the cytoplasmic and periplasmic sides
of the bacterial inner membrane, respectively.
Parts of the L, M, and H chains span the membrane,
whereas the cytochrome subunit sits on the periplasmic side, at the top.
The surface coloring ranges from dark goldenrod for the most hydrophobic
potentials, through white, to dark cyan for the most hydrophilic.
Ligands including lipid, detergent, heme, and various other cofactors
are shown as purple surfaces.
For image setup after the structure from OPM has been opened, see the command file mlp.cxc.
More features...Example Image
KCNQ1 is the pore-forming subunit of a cardiac potassium channel. It binds to calmodulin, and mutations in either of these proteins can cause congenital long QT syndrome, a dangerous propensity for irregular heartbeats. In the image, a structure of the KCNQ1/calmodulin complex (PDB 5vms) has been assembled into the native tetrameric form with the sym command. The view is from the cytoplasmic side, with KCNQ1 shown as surfaces, calmodulin as cartoons, and calcium ions as balls. A pastel palette from ColorBrewer has been used to color the surfaces, darkened with color modify for the cartoons, and “rotated” 45° in hue for the ions. See the command file colormod.cxc.
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