The three-dimensional structure of the asymmetric unit of the bundle has been determined using interproton distance restraints derived from the nuclear Overhauser effect (NOE), covalent torsion angle restraints derived from three bond scalar coupling constants, and longer range angular restraints derived from residual dipolar couplings. The 33-residue peptide, (α‘-SH), that is the basic building block of the bundle has been recombinantly expressed. The solution structure of a de novo designed disulfide-bridged two-α-helix peptide that self-assembles to form a 2-fold symmetric four-α-helix bundle protein (α‘-SS-α‘) 2 has been solved by NMR spectroscopy.
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