Tyrosine and tryptophan are noticeably rare in them, due primarily to their bulky side chains.
Tyrosine and tryptophan are noticeably rare in them, due primarily to their bulky side chains. Proline is the least prevalent amino acid in their structure, and its presence often disrupts their structure. First proposed in 1951 by Linus Pauling and Robert Corey, their structure is achieved by hydrogen bonding between the carbonyl and amine groups of every fourth amino acid residue. For ten points, identify this coiled component of protein secondary structure, the complement of the beta pleated sheet.
Tyrosine and tryptophan are noticeably rare in them, due primarily to their bulky side chains.
{Alpha Helix}