Centrosymmetric bilayers in the 0.75 A resolution structure of a designed alpha-helical peptide, D,L-Alpha-1.

@article{Patterson1999CentrosymmetricBI,
  title={Centrosymmetric bilayers in the 0.75 A resolution structure of a designed alpha-helical peptide, D,L-Alpha-1.},
  author={William R. Patterson and Daniel H. Anderson and William F. DeGrado and Duilio Cascio and David S Eisenberg},
  journal={Protein science : a publication of the Protein Society},
  year={1999},
  volume={8 7},
  pages={
          1410-22
        }
}
We report the 0.75 A crystal structure of a racemic mixture of the 12-residue designed peptide "Alpha-1" (Acetyl-ELLKKLLEELKG), the L-enantiomer of which is described in the accompanying paper. Equivalent solutions of the centrosymmetric bilayers were determined by two direct phasing programs in space groups P1 and P1bar. The unit cell contains two L-alpha-helices and two D-alpha-helices. The columnar-sheet bilayer motif seen in L-Alpha-1 is maintained in the D,L-Alpha-1 structure except that… CONTINUE READING
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