ArticleProceedings of the National Academy of Sciences of the United States of America2010
Extremely slow intramolecular diffusion in unfolded protein L.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- 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
- Theory on the Design Principles of Protein Molecular Oscillatory Machines.The journal of physical chemistry. B · 2025Article
- Zero- to low-field relaxometry of chemical and biological fluids.Communications chemistry · 2023Article
- Modeling Concentration-dependent Phase Separation Processes Involving Peptides and RNA via Residue-Based Coarse-Graining.Journal of chemical theory and computation · 2023Article
- Characterizing Transient Protein-Protein Interactions by Trp-Cys Quenching and Computer Simulations.The journal of physical chemistry letters · 2022Article
- Gradual compaction of the nascent peptide during cotranslational folding on the ribosome.eLife · 2020Article
- Slow Folding of a Helical Protein: Large Barriers, Strong Internal Friction, or a Shallow, Bumpy Landscape?The journal of physical chemistry. B · 2020Article
- N-Terminal Decarboxylation as a Probe for Intramolecular Contact Formation in γ-Glu-(Pro)The journal of physical chemistry. B · 2020Article
- Water as a Good Solvent for Unfolded Proteins: Folding and Collapse are Fundamentally Different.Journal of molecular biology · 2020Review
- Engineering Order and Cooperativity in a Disordered Protein.Biochemistry · 2019Article
- 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
- Microsecond sub-domain motions and the folding and misfolding of the mouse prion protein.eLife · 2019Article
- Position-, disorder-, and salt-dependent diffusion in binding-coupled-folding of intrinsically disordered proteins.Physical chemistry chemical physics : PCCP · 2019Article
- Intramolecular Diffusion in α-Synuclein: It Depends on How You Measure It.Biophysical journal · 2018Article
- Hypothesis: structural heterogeneity of the unfolded proteins originating from the coupling of the local clusters and the long-range distance distribution.Biophysical reviews · 2018Review
- Effects of maturation on the conformational free-energy landscape of SOD1.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Prion protein dynamics before aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Integrated view of internal friction in unfolded proteins from single-molecule FRET, contact quenching, theory, and simulations.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Monomer Dynamics of Alzheimer Peptides and Kinetic Control of Early Aggregation in Alzheimer's Disease.Chemphyschem : a European journal of chemical physics and physical chemistry · 2016Article
- Intramolecular diffusion controls aggregation of the PAPf39 peptide.Biophysical chemistry · 2016Article
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3 authors.
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Abstract
A crucial parameter in many theories of protein folding is the rate of diffusion over the energy landscape. Using a microfluidic mixer we have observed the rate of intramolecular diffusion within the unfolded B1 domain of protein L before it folds. The diffusion-limited rate of intramolecular contact is about 20 times slower than the rate in 6 M GdnHCl, and because in these conditions the protein is also more compact, the intramolecular diffusion coefficient decreases 100-500 times. The dramatic slowdown in diffusion occurs within the 250 micros mixing time of the mixer, and there appears to be no further evolution of this rate before reaching the transition state of folding. We show that observed folding rates are well predicted by a Kramers model with a denaturant-dependent diffusion coefficient and speculate that this diffusion coefficient is a significant contribution to the observed rate of folding.
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