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The '''beta hairpin''' (or '''beta-beta unit''') [[structural motif]] is the simplest [[protein]] motif involving two [[beta strand]]s that look like a [[hairpin]]. The motif consists of two strands that are adjacent in [[primary sequence]] oriented in an [[antiparallel]] arrangement (where the [[N-terminus]] of one sheet is adjacent to the [[C-terminus]] of the next) and linked by a short loop of two to five [[amino acid]]s. Beta hairpins can occur in isolation or as part of a series of [[hydrogen bond]]ed strands that collectively comprise a beta sheet. |
The '''beta hairpin''' (or '''beta-beta unit''') [[structural motif]] is the simplest [[protein]] motif involving two [[beta strand]]s that look like a [[hairpin]]. The motif consists of two strands that are adjacent in [[primary sequence]] oriented in an [[antiparallel]] arrangement (where the [[N-terminus]] of one sheet is adjacent to the [[C-terminus]] of the next) and linked by a short loop of two to five [[amino acid]]s. Beta hairpins can occur in isolation or as part of a series of [[hydrogen bond]]ed strands that collectively comprise a beta sheet. |
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As well as the[[α-helix|alfa helix]], this element of secondary structure can be formed in isolation by short linear peptides in solution, as shown by [[Blanco|Francisco J. Blanco]] and others. This suggests that hairpins could be initiation sites for [[protein folding]]. |
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{{Protein secondary structure}} |
{{Protein secondary structure}} |
Revision as of 21:52, 1 March 2007
![](https://upload.wikimedia.org/wikipedia/commons/thumb/b/ba/Beta_hairpin.png/220px-Beta_hairpin.png)
The beta hairpin (or beta-beta unit) structural motif is the simplest protein motif involving two beta strands that look like a hairpin. The motif consists of two strands that are adjacent in primary sequence oriented in an antiparallel arrangement (where the N-terminus of one sheet is adjacent to the C-terminus of the next) and linked by a short loop of two to five amino acids. Beta hairpins can occur in isolation or as part of a series of hydrogen bonded strands that collectively comprise a beta sheet. As well as thealfa helix, this element of secondary structure can be formed in isolation by short linear peptides in solution, as shown by Francisco J. Blanco and others. This suggests that hairpins could be initiation sites for protein folding.