The chemical evolution of four-α-helix bundle polypeptides to a flavoenzyme model was attempted by designing single-chain 53-peptides, which comprise flavin derivatives at three different positions. A pair of flavin derivatives were also introduced opposite to each other on the separate α-helix segments in the hydrophobic core. The four-α-helix bundle structure and the flavin moieties around the hydrophobic core were characterized by circular ...
[Slama, James T.; Radziejewski, Czestaw; Oruganti, SubbaRao; Kaiser, E. T. Journal of the American Chemical Society, 1984 , vol. 106, # 22 p. 6778 - 6785]
[Slama, James T.; Radziejewski, Czestaw; Oruganti, SubbaRao; Kaiser, E. T. Journal of the American Chemical Society, 1984 , vol. 106, # 22 p. 6778 - 6785]