期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 102, 期 50, 页码 17964-17968出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0507124102
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There is growing appreciation of the functional relevance of unfolded proteins in biology. However, unfolded states of proteins have proven inaccessible to the usual techniques for high-resolution structural and energetic characterization. Unfolded states are still generally conceived of as statistical coils, based on the pioneering work of Flory [(1969) Statistical Mechanics of Chain Molecules (Wiley, New York)] and Tanford [(1968) Adv. Protein Chem. 23, 121-282]. Recently, several lines of independent evidence have raised doubts about the random coil model and offer support for alternative views. Here, we show that polyproline II conformation is dominant in a host-guest peptide model AcGGXGGNH(2) (X not equal glycine), in equilibrium predominantly with beta-structure. This result is inconsistent with a random coil model and the general view that these peptides are unstructured. By calculating a set of apparent Delta G values from the measured coupling constants of the backbone amides, we can construct a polyproline II scale that correlates negatively with beta-sheet scales.
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