ArticleProceedings of the National Academy of Sciences of the United States of America2000
The Flory isolated-pair hypothesis is not valid for polypeptide chains: implications for protein folding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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Who cites it
91 citing papers in PubMed.
- Nearest-Neighbor Effects in Short Unfolded Peptides: An Assessment of Molecular Dynamics Force Fields.Journal of chemical information and modeling · 2026Article
- Nearest neighbour interactions between amino acid residues in short peptides and coil libraries.RSC advances · 2026Article
- 50 years in the shadow of the Ramachandran plot.Protein science : a publication of the Protein Society · 2025Article
- From isolated polyelectrolytes to star-like assemblies: the role of sequence heterogeneity on the statistical structure of the intrinsically disordered neurofilament-low tail domain.The European physical journal. E, Soft matter · 2024Article
- High-Accuracy Prediction of Stabilizing Surface Mutations to the Three-Helix Bundle, UBA(1), with EmCAST.Journal of the American Chemical Society · 2023Article
- Exploring Nearest Neighbor Interactions and Their Influence on the Gibbs Energy Landscape of Unfolded Proteins and Peptides.International journal of molecular sciences · 2022Review
- Randomizing of Oligopeptide Conformations by Nearest Neighbor Interactions between Amino Acid Residues.Biomolecules · 2022Article
- Protein folding - seeing is deceiving.Protein science : a publication of the Protein Society · 2021Article
- Why Proteins are Big: Length Scale Effects on Equilibria and Kinetics.The protein journal · 2019Review
- Experimentally Derived and Computationally Optimized Backbone Conformational Statistics for Blocked Amino Acids.Journal of chemical theory and computation · 2019Article
- Improvements to the ABSINTH Force Field for Proteins Based on Experimentally Derived Amino Acid Specific Backbone Conformational Statistics.Journal of chemical theory and computation · 2019Article
- Statistical description of the denatured structure of a single protein, staphylococcal nuclease, by FRET analysis.Biophysical reviews · 2018Article
- Anticooperative Nearest-Neighbor Interactions between Residues in Unfolded Peptides and Proteins.Biophysical journal · 2018Article
- Tuning the Flexibility of Glycine-Serine Linkers To Allow Rational Design of Multidomain Proteins.Biochemistry · 2017Article
- Conformational Heterogeneity and FRET Data Interpretation for Dimensions of Unfolded Proteins.Biophysical journal · 2017Article
- A closer look into the α-helix basin.Scientific reports · 2016Article
- Beyond basins: φ,ψ preferences of a residue depend heavily on the φ,ψ values of its neighbors.Protein science : a publication of the Protein Society · 2016Article
- The effect of chirality and steric hindrance on intrinsic backbone conformational propensities: tools for protein design.Protein engineering, design & selection : PEDS · 2016Article
- Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling.Chemical reviews · 2016Review
- Sequence- and Temperature-Dependent Properties of Unfolded and Disordered Proteins from Atomistic Simulations.The journal of physical chemistry. B · 2015Article
31 more citing papers are in PubMed but not listed here.
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3 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Using an all-atom representation, we exhaustively enumerate all sterically allowed conformations for short polyalanyl chains. Only intrachain interactions are considered, including one adjustable parameter, a favorable backbone energy (e.g., a peptide hydrogen bond). The counting is used to reevaluate Flory's isolated-pair hypothesis, the simplifying assumption that each phi,psi pair is sterically independent. This hypothesis is a conceptual linchpin in helix-coil theories and protein folding. Contrary to the hypothesis, we find that systematic local steric effects can extend beyond nearest-chain neighbors and can restrict the size of accessible conformational space significantly. As a result, the entropy price that must be paid to adopt any specific conformation is far less than previously thought.
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