| Abstract: | Many oligopeptide crystals show the β-pleated sheet structures. Both parallel and antiparallel chain pleated sheets are found, and also both ideal (flat) and heavily twisted sheets are found. The structural parameters, such as the T (NCα-C') angles, the torsion angles (φ and ø), the fiber axis periods, the hydrogen bond lengths, and the interchain spacings, are studied. Some of them deviate signifi cantly from those proposed by Pauling & Corey (Proc. Natl. Acad. Sci. US (1953), 39, 253–256). In the heavily twisted sheets, the twists are larger than those in the globular proteins, and each two neighboring chains are almost per pendicular with each other, preserving the β-sheet type hydrogen bond system. The torsion angles in the twisted sheets are rather close to those of the poly (L-proline) II helix. It also is discussed that the (NCαC) angles sometimes deviate by almost 5° from the standard value depending on the structures of the main and side chains. |
