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Perplexing cooperative folding and stability of a low-sequence complexity, polyproline 2 protein lacking a hydrophobic core
- Perplexing cooperative folding and stability of a low-sequence complexity, polyproline 2 protein lacking a hydrophobic core
- Gates, Zachary P.; Baxa, Michael C.; Yu, Wookyung; Riback, Joshua A.; Li, Hui; Roux, Benoit; Kent, Stephen B. H.; Sosnick, Tobin R.
- DGIST Authors
- Yu, Wookyung
- Issue Date
- Proceedings of the National Academy of Sciences of the United States of America, 114(9), 2241-2246
- Article Type
- Conference Paper
- Backbone; Collapse; Cooperativity; Cooperativity; Flea Antifreeze Protein; Free Energy; Hydrogen Bonds; Hydrogen Bonding; Hydrogen Bonding; Kinetics; Kinetics; Molecular Dynamics; Nonnative Interactions; Potential Functions; PP2; Protein Folding; Protein Folding; Transition State; Unfolded Proteins
- The burial of hydrophobic side chains in a protein core generally is thought to be the major ingredient for stable, cooperative folding. Here, we show that, for the snow flea antifreeze protein (sfAFP), stability and cooperativity can occur without a hydrophobic core, and without α-helices or β-sheets. sfAFP has low sequence complexity with 46% glycine and an interior filled only with backbone H-bonds between six polyproline 2 (PP2) helices. However, the protein folds in a kinetically two-state manner and is moderately stable at room temperature. We believe that a major part of the stability arises from the unusual match between residue-level PP2 dihedral angle bias in the unfolded state and PP2 helical structure in the native state. Additional stabilizing factors that compensate for the dearth of hydrophobic burial include shorter and stronger H-bonds, and increased entropy in the folded state. These results extend our understanding of the origins of cooperativity and stability in protein folding, including the balance between solvent and polypeptide chain entropies.
- National Academy of Sciences
- Related Researcher
Yu, Woo Kyung
Laboratory of Protein Biophysics
protein biophysics; protein folding; protein dynamics and conformational change
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