Issue Information

Abstract

Cover: In An and Lee et al. (http://doi.org/10.1002/cpps.92), the image shows the overall fold, Cβ-strip, and the 2D map of a β-barrel. (A) The cartoon representation of a β-barrel. The backbones are shown in sticks. The carbon, nitrogen, and oxygen atoms are colored in white, blue, and red, respectively. The side chains and hydrogen atoms are omitted for clarity. The backbone hydrogen bonds between strands are shown in yellow dashed lines. (B) A Cβ-strip is shown in sticks and cartoon representation in orange. The carbon, nitrogen, oxygen, and hydrogen atoms are colored in orange, blue, red, and white, respectively. (C) The 2D map of the β-barrel used in this article is shown in cartoon representation. Each circle represents a β-barrel residue. The strand residues are colored in white or gray, and the loop residues are colored in blue. An individual Cβ-strip is distinguished by gray or white color. One exemplary Cβ-strip is marked out with a gray dashed line. The last strand is also shown in dashed circles to show its complete hydrogen bond registry to the first strand. The N or C terminus of the protein is marked out by ‘N’ or ‘C’. The shear number (S) and strand distance (D) are marked out. Some of the N and C terminal residues in the actual blueprint file used in the article are omitted for clarity. Panels (A and B) are prepared using PyMOL (The PyMOL Molecular Graphics System, Schrödinger, LLC).