With no explanation, label text_A→text_B with either "not_related" or "related".
text_A: Anne Bancroft won a film award.
text_B: A Polyproline Helix is a type of protein secondary structure which occurs in proteins comprising repeating proline residues .. protein. protein. secondary structure. secondary structure. proline. proline. A left-handed polyproline II helix -LRB- PPII , poly-Pro II -RRB- is formed when sequential residues all adopt backbone dihedral angles of roughly -LRB- -75 ° , 150 ° -RRB- and have trans isomers of their peptide bonds .. trans. Cis–trans isomerism. This PPII conformation is also common in proteins and polypeptides with other amino acids apart from proline .. proline. proline. Similarly , a more compact right-handed polyproline I helix -LRB- PPI , poly-Pro I -RRB- is formed when sequential residues all adopt backbone dihedral angles of roughly -LRB- -75 ° , 160 ° -RRB- and have cis isomers of their peptide bonds .. cis. Cis–trans isomerism. Of the twenty common naturally occurring amino acids , only proline is likely to adopt the cis isomer of the peptide bond , specifically the X-Pro peptide bond ; steric and electronic factors heavily favor the trans isomer in most other peptide bonds .. proline. proline. trans. Cis–trans isomerism. peptide bond. peptide bond. cis. Cis–trans isomerism. However , peptide bonds that replace proline with another N-substituted amino acid -LRB- such as sarcosine -RRB- are also likely to adopt the cis isomer .. proline. proline. cis. Cis–trans isomerism. amino acid. amino acid. sarcosine. sarcosine
not_related.