This Indigo® alpha helix model consists of 20 amino acid cores that form a right handed or clockwise spiral. It shows protein secondary structure based on 3.6 amino acid residues per turn. This helical polypeptide backbone consists solely of alpha carbons and amino & carboxyl groups. The “R” groups are indicated with a univalent green atom & face outward where interact with other structures, e.g. the major groove of our 12 base pair DNA double helix model. It fits the major groove easily & shows steric hindrance compared to the minor groove..
The "R" groups can be augmented with additional parts to show the most commonly occurring amino acid residues methionine, alanine, leucine, glutamate and lysine in the alpha helix polypeptide chain. Alpha helices are common in important biological proteins such as keratin (skin), hemoglobin (blood) & myoglobin (muscle)
50mm bonds with white inserts represent hydrogen atoms that form hydrogen bonds. This makes it clearer how the alpha helix structure is kept stable through bonds (n to n+4) between the amide hydrogen of one amino acid and the carbonyl oxygen of another amino acid, 4 residues away in the amino acid sequence
|67288c||Bond, Minit, white, 210mm||1|
|68186-20||Wobbly bond, 20mm, each||100|
|68186-50||Wobbly bond, 50mm, each||17|
|68221C||Atom, Orbit, Cl "a", green, 1 prong||20|
|68227C||Atom, Orbit, O "b", 180 degree, red||20|
|68237C||Atom, Orbit, N "h", planar: 108-126-126, blue||20|
|68239C||Atom, Orbit, C "i", planar: 114-123-123, black||20|
|68244C||Atom, Orbit, C "k", tetrahedral, black||20|
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