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