Helix-sheet packing in proteins.

ABSTRACT: The three-dimensional structure of a protein is organized around the packing of its secondary structure elements. Although much is known about the packing geometry observed between alpha-helices and between beta-sheets, there has been little progress on characterizing helix-sheet interactions. We present an analysis of the conformation of alphabeta(2) motifs in proteins, corresponding to all occurrences of helices in contact with two strands that are hydrogen bonded. The geometry of the alphabeta(2) motif is characterized by the azimuthal angle theta between the helix axis and an average vector representing the two strands, the elevation angle psi between the helix axis and the plane containing the two strands, and the distance D between the helix and the strands. We observe that the helix

SUBMITTER: Hu C 

PROVIDER: S-EPMC2854864 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature