Helix-sheet packing in proteins

摘要: The three-dimensional structure of a protein is organized around the packing its secondary elements. While much known about geometry observed between α-helices and β-sheets, there has been little progress on characterizing helix-sheet interactions. We present an analysis conformation αβ2 motifs in proteins, corresponding to all occurrences helices contact with two strands that are hydrogen-bonded. motif characterized by azimuthal angle θ helix axis average vector representing strands, elevation ψ plane containing distance D strands. observe tends align preference for antiparallel orientation if parallel; this diminished other topologies β-sheet. Sidechain at interface mostly hydrophobic, aliphatic amino acids strand aromatic helix. From knowledge acid propensities we have derived different statistical potentials shown be efficient picking native-like conformations among set non-native well-known decoy datasets. information as well related applications field prediction.