ArticleProceedings of the National Academy of Sciences of the United States of America2017
Perplexing cooperative folding and stability of a low-sequence complexity, polyproline 2 protein lacking a hydrophobic core.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 40 citations in OpenAlex.
- PolyProline Predictor: A web server for empirical sequence-based prediction of polyproline II helices.Protein science : a publication of the Protein Society · 2026Article
- Protein Structure Determination by Racemic and Quasi-Racemic X-Ray Crystallography.Chembiochem : a European journal of chemical biology · 2026Review
- Sequence-Dependent Conformational Landscapes of Intrinsically Disordered Proteins Reveal Asymmetric Chain Compaction.Journal of chemical theory and computation · 2025Article
- The C-terminal tails of GroEL and its mitochondrial and chloroplastic homologs adopt polyproline II helices.Protein science : a publication of the Protein Society · 2025Article
- Orientation affects hydrogen bonding cooperativity in polyproline II helical bundles.Communications chemistry · 2025Article
- Amino Acid Residue-Specific Ramachandran Distributions Derived from a Simple Mean Field Potential.ACS physical chemistry Au · 2024Article
- Hydrogen bonding patterns and cooperativity in polyproline II helical bundles.Communications chemistry · 2024Article
- New insight into the mechanism by which antifreeze peptides regulate the physiological function of Streptococcus thermophilus subjected to freezing stress.Journal of advanced research · 2023Article
- Insight into polyproline II helical bundle stability in an antifreeze protein denatured state.Biophysical journal · 2022Article
- Do polyproline II helix associations modulate biomolecular condensates?FEBS open bio · 2021Review
- Piecewise All-Atom SMD Simulations Reveal Key Secondary Structures in Luciferase Unfolding Pathway.Biophysical journal · 2020Article
- Glycine in Water Favors the Polyproline II State.Biomolecules · 2020Article
- Water as a Good Solvent for Unfolded Proteins: Folding and Collapse are Fundamentally Different.Journal of molecular biology · 2020Review
- Predicting Conformational Properties of Intrinsically Disordered Proteins from Sequence.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Commonly used FRET fluorophores promote collapse of an otherwise disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Sequence Effects on Size, Shape, and Structural Heterogeneity in Intrinsically Disordered Proteins.The journal of physical chemistry. B · 2019Article
- Collapse Transitions of Proteins and the Interplay Among Backbone, Sidechain, and Solvent Interactions.Annual review of biophysics · 2018Article
- Peptide Solubility Limits: Backbone and Side-Chain Interactions.The journal of physical chemistry. B · 2018Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.