Alpha helix

The alpha helix (α-helix) is a common motif in the secondary structure of proteins and is a right hand-helix conformation 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. The alpha helix is also called a classic Pauling–Corey–Branson α-helix. The name 3.613-helix is also used for this type of helix, denoting the average number of residues per helical turn, with 13 atoms being involved in the ring formed by the hydrogen bond. Among types of local structure in proteins, the α-helix is the most regular and the most predictable from sequence, as well as the most prevalent.

Words

This table shows the example usage of word lists for keywords extraction from the text above.

WordWord FrequencyNumber of ArticlesRelevance
α-helix4140.358
helix57820.308
pauling–corey–branson210.216
alpha460410.19
helical23900.133

This website uses cookies to ensure you get the best experience on our website. Learn more. Got it.