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Protein Structural Analysis: Secondary Elements and Key Residue Mapping #238273 (License: Personal Use)

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3D protein structure diagram showing secondary elements (α-helices, β-sheets) and key residues (Asn113, Ala86, Glu121); panel A full fold, panel B close-up overlays.
JPG 956×1280 295.2 KB

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This image displays a eukaryotic protein’s tertiary structure, with α-helices in orange, red, green, and yellow; β-sheets in blue; and loops in cyan. Panel A highlights residue 119 in a boxed region, while Panel B overlays two structural states to compare side-chain orientations of Asn113, Ala86, Asp100, and Glu121. The N′ and C′ termini are labeled to indicate chain directionality.
Used in structural bioinformatics articles, molecular modeling tutorials, or enzyme mechanism explanations; targets researchers and students seeking visual insight into protein conformational changes and active-site residue roles.
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Related Cliparts: Visualize protein folding with detailed 3D models highlighting α-helices, β-sheets, and critical amino acid residues like Asn113 and Glu121 for structural biology research.

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