Beta sheet

Beta sheet
The β sheet (also β-pleated sheet) is a commonly occurring form of regular secondary structure in proteins, first proposed by Linus Pauling and Robert Corey in 1951.
Full article >>>

Secondary structure: highly patterned sub-structures - alpha helix and beta sheet - or segments of chain that assume no stable shape and are formed by hydrogen bonding.
Full article >>>

Another secondary structural element is called a "beta sheet" wherein the peptide backbone sort of traverses one direction, turns around and comes back, hydrogen bonding across as it moves.
Full article >>>

The N-terminal (residues 1-450) and C-terminal (residues 1050-1201) regions are predicted to form globular structures consisting of alternating alpha helices and beta sheets.
Full article >>>

alpha helix, beta sheet, random coil); local structure within an RNA molecule which is conferred by base pairing of nucleotides which are relatively closely positioned within the sequence (e.g., hairpins, stem-loop structures).
Full article >>>

a secondary structure that consists of a beta sheet.
They attack the outer surface of the cell membrane surrounding the pathogen eventually punching lethal holes in it.
Full article >>>

motif - A discrete portion of a protein assumed to fold independently of the rest of the protein and possessing its own function [from NCBI BLAST Guide Glossary]. Some common types of motifs are made up of two or more alpha helices or beta sheets.
Full article >>>


'"/>