ArticleChemical science2014
Folding Thermodynamics of Protein-Like Oligomers with Heterogeneous Backbones.
Article in Chemical science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Modulating thermal folded stability and catalytic activity of aRSC advances · 2026Article
- Manipulating the Unfolded State of a Folded Protein through Site-Specific Backbone Modification.Biochemistry · 2026Article
- Interplay between CChembiochem : a European journal of chemical biology · 2025Article
- Backbone Modification in a Protein Hydrophobic Core.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Article
- Site-directed allostery perturbation to probe the negative regulation of hypoxia inducible factor-1α.RSC chemical biology · 2024Article
- Effects of altered backbone composition on the folding kinetics and mechanism of an ultrafast-folding protein.Chemical science · 2024Article
- Chemical Shifts of Artificial Monomers Used to Construct Heterogeneous-Backbone Protein Mimetics in Random Coil and Folded States.Peptide science (Hoboken, N.J.) · 2023Article
- Implications of the unfolded state in the folding energetics of heterogeneous-backbone protein mimetics.Chemical science · 2022Article
- Vagabond: bond-based parametrization reduces overfitting for refinement of proteins.Acta crystallographica. Section D, Structural biology · 2021Article
- Analysis of folded structure and folding thermodynamics in heterogeneous-backbone proteomimetics.Methods in enzymology · 2021Review
- Proteomimetic surface fragments distinguish targets by function.Chemical science · 2020Article
- Proteomimetic Zinc Finger Domains with Modified Metal-binding β-Turns.Peptide science (Hoboken, N.J.) · 2020Article
- A twist in the road less traveled: The AMBER ff15ipq-m force field for protein mimetics.The Journal of chemical physics · 2020Article
- Impact of Substitution Registry on the Receptor-Activation Profiles of Backbone-Modified Glucagon-like Peptide-1 Analogues.Chembiochem : a European journal of chemical biology · 2019Article
- Heterogeneous-Backbone Foldamer Mimics of a Computationally Designed, Disulfide-Rich Miniprotein.Chembiochem : a European journal of chemical biology · 2019Article
- Thermodynamic Scale of β-Amino Acid Residue Propensities for an α-Helix-like Conformation.Journal of the American Chemical Society · 2018Article
- Foldamer Tertiary Structure through Sequence-Guided Protein Backbone Alteration.Accounts of chemical research · 2018Article
- Evaluation of β-Amino Acid Replacements in Protein Loops: Effects on Conformational Stability and Structure.Chembiochem : a European journal of chemical biology · 2018Article
- Advancing the Frontiers of Chemical Protein Synthesis-The 7Cell chemical biology · 2018Article
- Helix Propensities of Amino Acid Residues via Thioester Exchange.Journal of the American Chemical Society · 2017Article
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Authors and funding
2 authors.
Funding
Abstract
The thermodynamics of protein folding are dictated by a complex interplay of interatomic interactions and physical forces. A variety of unnatural protein-like oligomers have the capacity to manifest defined folding patterns. While the energetics of folding in natural proteins is well studied, little is known about the forces that govern folding in modified backbones. Here, we explore the thermodynamic consequences of backbone alteration on protein folding, focusing on two types of chemical changes made in different structural contexts of a compact tertiary fold. Our results reveal a surprising favorable impact on folding entropy that accompanies modifications that increase disorder in the ensemble of unfolded states, due to differences in the solvation of natural and unnatural backbones.
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