Solution structure of a diiron protein model: Due Ferri(II) turn mutant
Analysis and Design of Turns in alpha-Helical Hairpins
Solution characterization of diiron proteins containing two distinct types of inter-helical loops
Proton and metal ion-dependent assembly of a model diiron protein
Inaugural article: retrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteins
Preorganization of molecular binding sites in designed diiron proteins
Crystal structure of four-helix bundle model, Due Ferri(II) turn mutant
Crystal structure of four-helix bundle model
Solution structure of four-helix bundle model
This structure was determined using standard 2D homonuclear technique
structures with the least restraint violations, structures with the lowest energy
Torsion Angle Dynamics, Simulated Annealing, Energy Restrained Minimization
0.5mM protein concentration; 50mM phosphate buffer; 90% H2O, 10% D2O
Diiron proteins, four-helix bundle, protein design, inter-helical loops, DE NOVO PROTEIN