Multiple Choice
Why does poly-L-Glutamate adopt an α-helical structure at low pH but a random conformation above pH 5?
Why does poly-L-Glutamate adopt an α-helical structure at low pH but a random conformation above pH 5?
An α-helix would be destabilized most by:
At pH 6.8, which of the following peptides is least likely to form an α-helix?
Peptide # 1: RSEDNFGAPKSILWE Peptide # 2: DQKASVEMAVRNSGK
Why does proline often 'break' an alpha helix?