The Dundee Resource for Sequence Analysis and Structure Prediction. MacGowan SA, Madeira F et al. Protein Sci. 2020 Jan;29(1):277-297.
Cryo-EM structures of apo and antagonist-bound human Cav3.1. Zhao Y, Huang G et al. Nature. 2019 Dec 19;576(7787):492-497.
Experimental evidence of solvent-separated ion pairs as metastable states in electrostatic interactions of biological macromolecules. Yu B, Pettitt BM, Iwahara J. J Phys Chem Lett. 2019 Dec 19;10(24):7937-7941.
Structure and drug resistance of the Plasmodium falciparum transporter PfCRT. Kim J, Tan YZ et al. Nature. 2019 Dec 12;576(7786):315-320.
A generalized HIV vaccine design strategy for priming of broadly neutralizing antibody responses. Steichen JM, Lin YC et al. Science. 2019 Dec 6;366(6470):eaax4380.(Previously featured citations...)
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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, nonprofit, and personal use. Chimera is developed by the Resource for Biocomputing, Visualization, and Informatics (RBVI), supported in part by the National Institutes of Health (P41-GM103311).
UCSF ChimeraX (or simply ChimeraX) is the next-generation molecular visualization program from the RBVI, following UCSF Chimera.
The default ribbon path is a smooth bspline (semitransparent tan in the figure), which can diverge from the true positions of the backbone atoms (α-carbons shown as gray balls). A cardinal spline allows tracking the backbone more closely. Without smoothing (light blue), it follows the α-carbons exactly, or it can be combined with some “compromise” smoothing of strand and/or coil. Ribbon spline options can be set with the ribspline command or in the molecule model attributes.(More features...)
Thermosomes are hollow balls inside which proteins are folded. They are found in the cytosol of eukaryotes and in archaea. Eukaryotic thermosomes have 8 different protein subunits, while archaeal ones are composed of one, two or three different proteins. The one shown from Thermoplasma acidophilum has two distinct proteins colored blue and yellow, each present in 8 copies. The two proteins have 60% sequence identity and are very similar in structure. One monomer is shown as a ribbon. Actin and tubulin are folded by eukaryotic thermosomes.
Protein Data Bank model 1a6d.(More samples...)
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