GF results and structural analyses of five peptides. (top) GF analysis of peptides. The purified peptides were loaded onto the Superdex G75 column in a buffer solution of 20 mM Tris-HCl, pH 8.0. The peak molecular mass was estimated by comparison with the protein standards running on the same column. The clear peak of gHH1 occurred at about 12.1 kDa. This molecular mass matches the approximate sum of four molecules, indicating the formation of the homotetrameric structure. The peak of gHH2 occurred at about 7.2 kDa, indicating the formation of the homodimeric structure. The peak of gHH3 occurred at about 3.8 kDa, indicating the monomeric state. The peak of gHH5 occurred at about 9.1 kDa, indicating the formation of the homotrimeric structure. The peak of gBH1 occurred at about 10.7 kDa, indicating the formation of the homotrimeric structure. (bottom) Sequences and calculated oligomeric states of gHH1, gHH2, gHH3, gHH5, and gBH1 in aqueous solution.
Wang et al. Virology Journal 2011 8:190 doi:10.1186/1743-422X-8-190