-Helical secondary structure occurs widely in globular proteins and its formation is a key step in their folding. As a consequence, understanding the energetics of helix formation is crucial to understanding protein folding and stability. We have measured the helix propensities of the nonpolar amino acids for an α-helix in an intact protein, ribonuclease T_1, and for a 17-residue peptide with a sequence identical to that of the α-helix in the protein. The helix propensities are in excellent agreement.
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