A designed four helix bundle protein with native-like structure.

摘要: A 108 amino acid protein was designed and constructed from a reduced alphabet of seven acids. The 2.9 resolution X-ray crystal structure confirms that the is four helix bundle, as it to be. Hydrogen/deuterium exchange experiments reveal buried amide protons with protection factors in excess 1 × 106 range characteristic well protected functional folded proteins (103–108) rather than rapid (0–102). monomeric at mM, concentration which were undertaken, indicating are due unique stable tertiary fold, not any higher order quaternary structure. Thermodynamic analysis provides an estimate free energy folding −9.3 kcal mole−1 25 °C, consistent derived most protons, global unfolding required for protons.