The human c-subunit of F1F~_o-ATP synthase is comprised of 75 amino acid residues (DIDTAAKFIG AGAATVGVAG SGAGIGTVFG SLIIGYARNP SLKQQLFSYA ILGFALSEAM GLFCLMVAFL ILFAM, MW 7608) and contains two transmembrane helices. The multimeric c-subunits assemble into ring-like architecture in membranes that functions as a rotary proton-channel for F~o-proton motor. We previously reported on the synthesis of a csubunit of is. coli F1F)o-ATP synthase, which was accomplished by means of the thioester method [1]. However, little is known concerning the structural details of c-subunit of human F1F_o-ATP synthase (Sub.c) due to the inherent difficulties in producing, handling and purifying the protein. Large scale methods for the isolation and purification of human Sub.c by molecular biology techniques have not yet been achieved. Here we report on the status of our studies on the chemical synthesis of human Sub.c. The study largely involved elucidating the structure-function relationships of ATP synthase using solution and solid-state NMR techniques.
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