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How are alpha helix structures of proteins stabilized?

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The alpha helix is a rod like structure. A tightly coiled backbone forms the inner part of the rod and the side chain extends outwards in a helical manner. read more

The alpha helix is a rod like structure. A tightly coiled backbone forms the inner part of the rod and the side chain extends outwards in a helical manner. The alpha helix is stabilized by hydrogen bonds between the NH and CO groups of the main chain I.e the CO group of each aminoacids forms a H-bond with the NH group of the amino acid I.e situated four residues ahead in the sequence..hope this is clear. read more

The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a righthand-spiral conformation (i.e. helix) in which every backbone N−H group donates a hydrogen bond to the backbone C=O group of the amino acid located three or four residues earlier along the protein sequence. read more

An α-helix is generally stabilized by amino acids in the primary structure with uncharged side chains, and, although there is some debate, it may be destabilized by those with bulky or charged side chains (Chapter 2, see Fig. 2-1). read more

The α-helix is not the only helical structure in proteins. Other helical structures include the 3_10 helix, which is stabilized by hydrogen bonds of the type (i, i+3) and the π-helix, which is stabilized by hydrogen bonds of the type (i, i+5). The 3_10 helix has a smaller radius, compared to the α-helix, while the π-helix has a larger radius. read more

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