Angewandte Chemie · 2000 · 88 citations · 18 references
Life SciencesBiochemistryMolecular BiologyProtein BiochemistryProtein EngineeringStructural BiologyCombinatorial Peptide SynthesisMacromolecular AssemblyMacromolecular StructureProtein Complex AssemblyProtein ConformationProtein StructureAmino AcidsCombinatorial Cyclic Peptide SynthesisCyclic Peptide LibrariesHelical ConformationPeptide Self-assemblyProtein Self-assemblyRedox PotentialRedox Potential Changes
De novo proteins were assembled from two sets of helical peptides on cyclic peptide templates bound to cellulose membranes (see picture). The variation of the amino acids of the hydrophobic binding pocket in the antiparallel four-helix bundle tuned the redox potential of the reversibly bound Fe(III) - protoporphyrin IX group, as directly detected spectroscopically on the solid support.
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Design and synthesis of multi-haem proteins
Dan E. Robertson, Ramy Farid, Christopher C. Moser et al. · Nature · 1994 · 571 citations