Hydrogen bonding in parallel and antiparallel beta sheets in globular

These hydrogen bonds provide the major attractive force which maintains the sheet structure. Phi and psi values that permit this alignment in antiparallel sheets have of -139° and +135°, respectively. The median values for a parallel sheet are -119° and +113°. Twisted sheets are found in globular proteins.

Draw the Hydrogen bonds that occur in the following alpha helix and beta sheet structures, and label the beta sheets that are parallel and anti-parallel: :0 0: Get more help from Chegg Get 1:1 help now from expert Biology tutorsIn the heavily twisted sheets, the twists are large than those in the globular proteins, and each two neighboring chains are almost perpendicular with each other, preserving the beta-sheet type hydrogen bond system. The torsion angles in the twisted sheets are rather close to those of the poly (L-proline) II helix.

Hydrogen bonds in beta sheets are on average 0.1 Angstroms shorter than those found in alpha helices. Beta sheets are designated as parallel or antiparallel based on the relative direction of the two interacting beta strands. The average length of a beta sheet is about 6 residues and most beta sheets contain fewer than 6 strands. The side chains of the amino acids of a strand in a beta sheet are found on opposite sides of the sheet and don't interact with one another. Therefore, like alpha ... A protein configuration resulting from the alignment of multiple adjacent beta strands and formation of hydrogen bonds between them. The beta sheet is a major secondary protein structure motif elucidated by Pauling and Corey, which consists of polypeptide chains in sheets laid side-by-side and are almost completely extended, with an axial ...antiparallel beta pleated sheets this is a secondary structure where neighboring hydrogen bonded polypeptides rin in oppostie directions allows for a stronger hydrogen bond d/t direct contactBeta hairpins are one of the simplest, and most abundant (in globular proteins), supersecondary structures involving beta sheets Figure 4.0 and Figure 4.1 shows that the hairpin consists of two antiparallel beta strands connected by a loop and as its name suggests it looks like a hair pin!

The hydrogen bond between these groups help stablized the beta sheet. (NOTE: in most pdb files, the locations of the hyrdrogen atoms are not shown). Every peptide group in the seet is involved in similar hydrogen bond so a repeating network of hydrogen bonds forms along the plane of the sheet to stabilize the structure.However, unlike alphas helices, the hydrogen bonds that hold beta pleated sheets together are perpendicular to the direction of the sheets. In the video I draw beta pleated sheets running parallel ...The beta pleated sheet occurs when two or more regions of the polypeptide lying side by side are connected by hydrogen bonds between parts of the two parallel polypeptide portions.