<molecular biology> A particular helical folding of the polypeptide backbone in protein molecules (both fibrous and globular), in which the carbonyl oxygens are all hydrogen bonded to amide nitrogen atoms three residues along the chain. ... The translation of amino acid residues along the long axis is 0.15 nm and the rotation per residue, 100...
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Frequently highly stable protein chain conformation stabilised by hydrogen bonding between peptide groups and having side chains projecting outwards in a spiral (3.6 residues per turn). One of the classic 'secondary' structures. Has end to end dipole because of alignment of peptide carbonyl groups
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(= a-helix) A particular helical folding of the polypeptide backbone in protein molecules (both fibrous and globular), in which the carbonyl oxygens are all hydrogen-bonded to amide nitrogen atoms three residues along the chain. The translation of amino acid residues along the long axis is 0.15nm, and the rotation per residue, 100°, so that there are 3.6 residues per turn.
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Alpha helix: The coiled structure of many proteins consisting of a single chain of amino acids stabilized by hydrogen bonds. The alpha helix was first proposed by Linus Pauling and Robert Corey in a brilliant series of paper in the early 1950s. It is also known as the Pauling-Corey helix. See also: Pauling, Linus. Common Misspellings: alpa helix
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the rodlike spatial configuration of many protein molecules in which the polypeptide backbone is stabilized by hydrogen bonds between amino acids in successive helical turns.
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