Search results
Results From The WOW.Com Content Network
The beta sheet (β-sheet, also β-pleated sheet) is a common motif of the regular protein secondary structure. Beta sheets consist of beta strands ( β-strands ) connected laterally by at least two or three backbone hydrogen bonds , forming a generally twisted, pleated sheet.
Protein secondary structure is the local spatial conformation of the polypeptide backbone excluding the side chains. [1] ... E = (Extended) strand of a β-pleated sheet;
Alpha sheet (also known as alpha pleated sheet or polar pleated sheet) is an atypical secondary structure in proteins, first proposed by Linus Pauling and Robert Corey in 1951.
The beta sheet is anti-parallel, and alternate strands run in the same directions. The first strand and last strand are next to each other and bonded by hydrogen bonds. Connecting loops can be long and include other secondary structures. The Greek key motif has its name because the structure looks like the pattern seen on Greek urns.
Secondary structure refers to highly regular local sub-structures on the actual polypeptide backbone chain. Two main types of secondary structure, the α-helix and the β-strand or β-sheets, were suggested in 1951 by Linus Pauling. [5] These secondary structures are defined by patterns of hydrogen bonds between the main-chain peptide groups.
Secondary structure [4] [5] α-Helices Cylindrical spiral ribbons, with ribbon plane approximately following plane of peptides. β-Strands Arrows with thickness, about one-quarter as thick as they are wide, showing direction and twist of the strand from amino to carboxy end. β-sheets are seen as unified because neighboring strands twist in unison.
The immunoglobulin domain, also known as the immunoglobulin fold, is a type of protein domain that consists of a 2-layer sandwich of 7-9 antiparallel β-strands arranged in two β-sheets with a Greek key topology, [1] [2] consisting of about 125 amino acids. The backbone switches repeatedly between the two β
Moreover, the typical secondary structure prediction methods do not account for the influence of tertiary structure on formation of secondary structure; for example, a sequence predicted as a likely helix may still be able to adopt a beta-strand conformation if it is located within a beta-sheet region of the protein and its side chains pack ...