ArticleProceedings of the National Academy of Sciences of the United States of America2006
End-to-end distance distributions and intrachain diffusion constants in unfolded polypeptide chains indicate intramolecular hydrogen bond formation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 104 papers.
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104 citing papers in PubMed.
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- 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
- Structural biases in disordered proteins are prevalent in the cell.Nature structural & molecular biology · 2024Article
- Fluorescence-readout as a powerful macromolecular characterisation tool.Chemical science · 2023Review
- Local and Large-Scale Conformational Dynamics in Unfolded Proteins and IDPs. II. Effect of Temperature and Internal Friction.The journal of physical chemistry. B · 2023Article
- Local and Large-Scale Conformational Dynamics in Unfolded Proteins and IDPs. I. Effect of Solvent Viscosity and Macromolecular Crowding.The journal of physical chemistry. B · 2023Article
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- Quantitative Elasticity of Flexible Polymer Chains Using Interferometer-Based AFM.Nanomaterials (Basel, Switzerland) · 2022Article
- Coarse-Grained Simulations of Protein Folding: Bridging Theory and Experiments.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Glycine-Rich Peptides from FUS Have an Intrinsic Ability to Self-Assemble into Fibers and Networked Fibrils.Biochemistry · 2021Article
- Highly Emissive Biological Bilirubin Molecules: Shedding New Light on the Phototherapy Scheme.The journal of physical chemistry. B · 2021Article
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- Automated and optimally FRET-assisted structural modeling.Nature communications · 2020Article
- Protein structural changes characterized by high-pressure, pulsed field gradient diffusion NMR spectroscopy.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020Article
- Emerging consensus on the collapse of unfolded and intrinsically disordered proteins in water.Current opinion in structural biology · 2020Review
- Intrinsically disordered proteins of viruses: Involvement in the mechanism of cell regulation and pathogenesis.Progress in molecular biology and translational science · 2020Review
- The Influence of Molecular Reach and Diffusivity on the Efficacy of Membrane-Confined Reactions.Biophysical journal · 2019Article
44 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Characterization of the unfolded state is essential for the understanding of the protein folding reaction. We performed time-resolved FRET measurements to gain information on the dimensions and the internal dynamics of unfolded polypeptide chains. Using an approach based on global analysis of data obtained from two different donor-acceptor pairs allowed for the determination of distance distribution functions and diffusion constants between the chromophores. Results on a polypeptide chain consisting of 16 Gly-Ser repeats between the FRET chromophores reveal an increase in the average end-to-end distance from 18.9 to 39.2 Angstrom between 0 and 8 M GdmCl. The increase in chain dimensions is accompanied by an increase in the end-to-end diffusion constant from (3.6 +/- 1.0) x 10(-7) cm(2) s(-1) in water to (14.8 +/- 2.5) x 10(-7) cm(2) s(-1) in 8 M GdmCl. This finding suggests that intrachain interactions in water exist even in very flexible chains lacking hydrophobic groups, which indicates intramolecular hydrogen bond formation. The interactions are broken upon denaturant binding, which leads to increased chain flexibility and longer average end-to-end distances. This finding implies that rapid collapse of polypeptide chains during refolding of denaturant-unfolded proteins is an intrinsic property of polypeptide chains and can, at least in part, be ascribed to nonspecific intramolecular hydrogen bonding. Despite decreased intrachain diffusion constants, the conformational search is accelerated in the collapsed state because of shorter diffusion distances. The measured distance distribution functions and diffusion constants in combination with Szabo-Schulten-Schulten theory were able to reproduce experimentally determined rate constants for end-to-end loop formation.
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