. "The complete resonance assignment of the ColE1 rop (rom) protein at pH 2.3 was obtained by two-dimensional (2D) proton nuclear magnetic resonance spectroscopy (1H NMR) at 500 and 600 MHz using through-bond and through-space connectivities. Sequential assignments and elements of regular secondary structure were deduced by analysis of nuclear Overhauser enhancement spectroscopy (NOESY) experiments and 3JHN alpha coupling constants. One 7.2-kDa monomer of the homodimer consists of two antiparallel helices connected by a hairpin loop at residue 31. The C-terminal peptide consisting of amino acids 59-63 shows no stable conformation. The dimer forms a four-helix bundle with opposite polarization of neighboring elements in agreement with the X-ray structure." . . . "Biochemistry" . "Sander C." . "Eberle W." . "Cesarini G." . "Klaus W." . "Roesch P." . "1990"^^ . "7402-7407" . "Proton nuclear magnetic resonance assignments and secondary structure determination of the ColE1 rop (rom) protein." . "29" . "doi:10.1021/bi00484a007" . . .