4hb1
From Proteopedia
|
A DESIGNED FOUR HELIX BUNDLE PROTEIN.
Overview
A 108 amino acid protein was designed and constructed from a reduced, alphabet of seven amino acids. The 2.9 A resolution X-ray crystal, structure confirms that the protein is a four helix bundle, as it was, designed to be. Hydrogen/deuterium exchange experiments reveal buried, amide protons with protection factors in excess of 1 x 10(6) in the range, characteristic of well protected protons in functional folded proteins, (10(3)-10(8)) rather than protons in rapid exchange (0-10(2)). The protein, is monomeric at 1 mM, the concentration at which the exchange experiments, were undertaken, indicating that the exchange factors are due to a unique, stable tertiary structure fold, and not due to any higher order quaternary, structure. Thermodynamic analysis provides an estimate of the free energy, of folding of -9.3 kcal mole-1 at 25 degrees C, consistent with the free, energy of folding derived from the protection factors of the most, protected protons, indicating that global unfolding is required for, exchange of the most protected protons.
About this Structure
4HB1 is a Protein complex structure of sequences from Synthetic construct with as ligand. Full crystallographic information is available from OCA.
Reference
A designed four helix bundle protein with native-like structure., Schafmeister CE, LaPorte SL, Miercke LJ, Stroud RM, Nat Struct Biol. 1997 Dec;4(12):1039-46. PMID:9406555
Page seeded by OCA on Tue Jan 29 21:46:33 2008
