A direct comparison of helix propensity in proteins and peptides.
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ABSTRACT:
SUBMITTER: Myers JK
PROVIDER: S-EPMC20282 | biostudies-literature | 1997 Apr
REPOSITORIES: biostudies-literature
Publications
A direct comparison of helix propensity in proteins and peptides.
Myers J K JK Pace C N CN Scholtz J M JM
Proceedings of the National Academy of Sciences of the United States of America 19970401 7
alpha-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 alpha-helix in an intact protein, ribonuclease T1, and for a 17-residue peptide with a sequence identical to that of the alpha-helix in the protein. The helix propensities are in ex ...[more]
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