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Ankyrin Repeat Protein Structure - Molecular Visualization of Repeats 1, 5, and 6 #1390562 (License: Personal Use)
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Panel (a) displays ankyrin repeat 1 with blue α-helices and red β-turns, featuring critical residues K303, R302, D75, and H84 involved in stabilization. Panel (b) shows repeats 5 (orange) and 6 (yellow-green) with extended helical bundles and salt bridges (e.g., R253-D226, R218-D243), illustrating how conserved motifs enable modular protein interaction surfaces.
Used in molecular biology and structural bioinformatics resources to explain ankyrin repeat architecture, domain engineering, or disease-associated mutations; targets researchers, students, and clinicians seeking mechanistic insights into scaffold proteins like ANKRD1 or NF-κB regulators.
Related Cliparts: Detailed 3D structural visualization of ankyrin repeats 1, 5, and 6, highlighting key amino acid residues, hydrogen bonding, and conserved folding motifs essential for protein-protein interactions.
(view all Ankyrin Repeat Protein Structure - Molecular Visualization of Repeats 1, 5, and 6)
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