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<p>state and by removing enthalpically stabilized "decoy" folds that compete with the fully helical state. It has been shown that ?-helices are more stable, robust to mutations and designable than ?-strands in natural proteins, and also in artificially designed proteins.</p>

<p><a href="page.php?w=Image%3AHelix_electron_density_myoglobin_2nrl_17-32.jpg">thumb</a></p>

<p><big> Visualization </big></p>
<p>The three most popular ways of visualizing the alpha-helical secondary structure of oligopeptide sequences are (1) a <a href="page.php?w=helical_wheel">helical wheel</a>,</p><p>
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