beta hairpin

In aqueous solution Arenicin-3 takes on a beta hairpin structure.

Beta hairpins are broken into four distinct classes as shown in the figure below.

This pattern continues indefinitely and defines all beta hairpins within the class.

Arenicin-1 is composed of 21 amino acids with a beta hairpin structure.

Researchers used the results of this study to identify a beta hairpin that was a major source of molecular interactions within the structure.

Arenicin-2 is a 21 amino acid peptide with a beta hairpin structure in aqueous solution.

This hairpin has sequence features similar to over 13,000 known hairpins, and thus may serve as a more general model for beta hairpin formation.

Studies of a beta hairpin called chignolin have uncovered a stepwise folding process that drives beta-hairpin folding.

The tertiary structure of the CH finger consists of a beta hairpin folded against an alpha helix.

As substitutions are the most common amino acid mutations, a protein could potentially undergo a conversion without affecting the functionality of the beta hairpin.

Beta hairpins can occur in isolation or as part of a series of hydrogen bonded strands that collectively comprise a beta sheet.

The FYVE domain is composed of two small beta hairpins (or zinc knuckles) followed by an alpha helix.

Beta hairpins were originally categorized solely by the number of amino acid residues in their loop sequences, such that they were named one-residue, two-residue, etc.

Beta barrels generally consist of at least one Greek key structural motif linked to a beta hairpin, or two successive Greek keys.

The beta hairpin (sometimes also called beta-ribbon or beta-beta unit) is a simple protein structural motif involving two beta strands that look like a hairpin.

The C-terminal domain, has 3 beta strands and two protrusions; one of which is a C-terminal alpha helix, and the second is a beta hairpin.

CV-N has a complex fold composed of a duplication of a tandem repeat of two homologous motifs comprising three-stranded beta sheet and beta hairpins.

The structure is amphiphilic with a nonuniform surface distribution of positive charge and contains several key structural elements, including a triple-stranded, antiparallel beta sheet with strands 2 and 3 in a beta hairpin conformation.