Assignment of backbone 1H, 13C and 15N resonances of human IgG1 Fc (51.4 kDa)

Here we report the NMR resonance assignments for the Fc region of human IgG1 expressed in E. coli, a 51.4 kDa dimer in solution (residues 221–447). The assignments have been deposited in the BioMagResBank with a BMRB accession number of 15514.     

Assignment of the 1H, 13C and 15N resonances of the calponin homology-2 domain of α-actinin-4

We report the assignment of the 110 amino acid second calponin homology domain of human α-actinin-4. The two calponin homology domains of α-actinin combine to regulate F-actin binding.     

Letter to the Editor: Backbone 1H, 15N and 13C Assignments for the Subunit a of the E. Coli ATP Synthase

The structure of the 30 KDa subunit a of the membrane component (F(0)) of E. coli ATP synthase is investigated in a mixture of chloroform, methanol and water, a solvent previously used for solving the structure of another integral membrane protein, subunit c. Near complete backbone chemical shift assignments were made from a set of TROSY experiments including HNCO, HNCA, HN(CA)CB, HN(CO)CACB and 4D HNCOCA and HNCACO. Secondary structure of subunit a was predicted from the backbone chemical shifts using TALOS program. The protein was found to consist of multiple elongated alpha-helical segments. This finding is generally consistent with previous predictions of multiple transmembrane alpha-helices in this polytopic protein.