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This topic has appeared in the trending rankings 1 time(s) in the past year. While it does not trend frequently, its appearance suggests a renewed or concentrated surge of public interest.
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Leucine_zipper entered the ranking for the first time today at position #. This is its highest position ever recorded.
This topic has appeared in the English Wikipedia rankings 1 time. It first appeared on 2026-03-30 and was most recently seen on 2026-03-30.
A leucine zipper is a common three-dimensional structural motif in proteins. It was first described by Landschulz and collaborators in 1988 when they found that an enhancer binding protein had a very characteristic 30-amino acid segment, and the display of these amino acid sequences on an idealized alpha helix revealed a periodic repetition of leucine residues at every seventh position over a distance covering eight helical turns. The polypeptide segments containing these periodic arrays of leucine residues were proposed to exist in an alpha-helical conformation and the leucine side chains from one alpha helix interdigitate with those from the alpha helix of a second polypeptide, facilitating dimerization.
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