Structural characteristics and stabilizing principles of bent β‐strands in protein tertiary architectures

Abstract

β‐Strands as constituents of β‐pleated sheets in protein tertiary structures often display considerable distortion from a purely extended conformation. The dislocation types are often characterized as “bulging,” “twisting,” and “bending.” The former 2 properties have been extensively studied and classified. In this work an investigation of bent β‐structures is undertaken. The structural characteristics examined included the bending angles within and out of the principal strand plane, their distribution among various strand types such as parallel and antiparallel, the amino acid preferences at bend sites, and the usage of charged and polar residues for stabilization through interactive anchoring with other atoms of the β‐sheet within which the bent strand lies. Copyright © 1994 The Protein Society