text: Yo, check it out, we 'bout to investigate
  The specificity of anti H1 antibodies, straight
  Peptides from the N- and C-domain of H1
  And the synthetic oligonucleotide, (AT)6, what they gonna do?
  
  Circular dichroism (CD) spectroscopy revealed
  That the free peptides H1(1-16), H1(204-218), and C(121-210) sealed
  In low salt buffer, they got a random structure, that's the deal
  But they turn helical when they bind to the oligonucleotide, for real
  
  Enzyme linked immunosorbent assay (ELISA), it's the test
  With anti-H1 antibodies in SLE patients, we invest
  And the monoclonal anti-H1 antibody MRA-12, the best
  Derived from MLR lpr/lpr autoimmune mice, no jest
  
  Binding of these antibodies to H1(204-218) and C, hold on tight
  Inhibited by 50% when these H1 peptides unite
  With (AT)6, the oligonucleotide shining bright
  But when tested with H1 fragment GC(34-210), it's a different sight
  
  No influence on antibody binding, it's not affected
  Even when H1 is bound to (AT)6, it's not neglected
  Competition studies with liquid phase GC and C, we selected
  Against solid phase GC and C, which one's respected?
  
  Liquid phase GC, it's more efficient, no denying
  Displacing antibody binding reactivity, it's satisfying
  More than liquid phase C, that's the truth, no lying
  But both liquid phase antigens against solid phase C, they're defying
  
  So we conclude, anti-H1 autoantibodies ain't playin'
  They target an epitope near the G- and C-domain, no delaying
  Exposed and unmasked when H1 is bound to DNA, no betraying
  That's the knowledge we gain from this scientific displaying