ArticleScience (New York, N.Y.)2015
Structural origin of slow diffusion in protein folding.
Article in Science (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.
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Who cites it
89 citing papers in PubMed, 210 citations in OpenAlex.
- Cooperative Native Contact Formation Facilitates Free Energy Barrier Crossing in Protein Folding.Physical review letters · 2026Article
- Static and dynamic rough energy landscapes can lead to identical diffusivity.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Resolving Molecular Interactions in Protein Folding Trajectories with NCIPLOT.Journal of chemical information and modeling · 2025Article
- Subdiffusion from competition between multi-exponential friction memory and energy barriers.The European physical journal. E, Soft matter · 2025Article
- Three-color single-molecule maximum likelihood analysis of folding and binding of diffusing molecules.Biophysical journal · 2025Article
- Model-free photon analysis of diffusion-based single-molecule FRET experiments.Nature communications · 2025Article
- GōMartini 3: From large conformational changes in proteins to environmental bias corrections.Nature communications · 2025Article
- A Stochastic Landscape Approach for Protein Folding State Classification.Journal of chemical theory and computation · 2024Article
- The role of memory-dependent friction and solvent viscosity in isomerization kinetics in viscogenic media.Nature communications · 2024Article
- Activation and friction in enzymatic loop opening and closing dynamics.Nature communications · 2024Article
- Electrostatics and hydrophobicity in the dynamics of intrinsically disordered proteins.The European physical journal. E, Soft matter · 2023Article
- Time-resolved burst variance analysis.Biophysical reports · 2023Article
- Fast protein folding is governed by memory-dependent friction.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Analytical Flory Random Coil Is a Simple-to-Use Reference Model for Unfolded and Disordered Proteins.The journal of physical chemistry. B · 2023Article
- Robust membrane protein tweezers reveal the folding speed limit of helical membrane proteins.eLife · 2023Article
- The analytical Flory random coil is a simple-to-use reference model for unfolded and disordered proteins.bioRxiv : the preprint server for biology · 2023Article
- Theory and Analysis of Single-Molecule FRET Experiments.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Observing the base-by-base search for native structure along transition paths during the folding of single nucleic acid hairpins.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The A39G FF domain folds on a volcano-shaped free energy surface via separate pathways.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Integrating single-molecule spectroscopy and simulations for the study of intrinsically disordered proteins.Methods (San Diego, Calif.) · 2021Article
29 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 4 institutions in 1 country.
Funding
Abstract
Experimental, theoretical, and computational studies of small proteins suggest that interresidue contacts not present in the folded structure play little or no role in the self-assembly mechanism. Non-native contacts can, however, influence folding kinetics by introducing additional local minima that slow diffusion over the global free-energy barrier between folded and unfolded states. Here, we combine single-molecule fluorescence with all-atom molecular dynamics simulations to discover the structural origin for the slow diffusion that markedly decreases the folding rate for a designed α-helical protein. Our experimental determination of transition path times and our analysis of the simulations point to non-native salt bridges between helices as the source, which provides a quantitative glimpse of how specific intramolecular interactions influence protein folding rates by altering dynamics and not activation free energies.
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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.