ArticleBiophysical journal2009
Direct observation of downhill folding of lambda-repressor in a microfluidic mixer.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 38 citations in OpenAlex.
- Advances in Mixer Design and Detection Methods for Kinetics Studies of Macromolecular Folding and Binding on the Microsecond Time Scale.Molecules (Basel, Switzerland) · 2022Article
- Predicting and Simulating Mutational Effects on Protein Folding Kinetics.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Slow Folding of a Helical Protein: Large Barriers, Strong Internal Friction, or a Shallow, Bumpy Landscape?The journal of physical chemistry. B · 2020Article
- Entropic Control of an Excited Folded-Like Conformation in a Disordered Protein Ensemble.Journal of molecular biology · 2018Article
- Protein unfolding mechanisms and their effects on folding experiments.F1000Research · 2017Review
- When fast is better: protein folding fundamentals and mechanisms from ultrafast approaches.The Biochemical journal · 2016Review
- Cooperative folding near the downhill limit determined with amino acid resolution by hydrogen exchange.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Resolution of Two Sub-Populations of Conformers and Their Individual Dynamics by Time Resolved Ensemble Level FRET Measurements.PloS one · 2015Article
- Complex pathways in folding of protein G explored by simulation and experiment.Biophysical journal · 2014Article
- Fast protein folding kinetics.Quarterly reviews of biophysics · 2014Review
- Observation of complete pressure-jump protein refolding in molecular dynamics simulation and experiment.Journal of the American Chemical Society · 2014Article
- Dodine as a protein denaturant: the best of two worlds?The journal of physical chemistry. B · 2013Article
- Microsecond folding experiments and simulations: a match is made.Physical chemistry chemical physics : PCCP · 2013Article
- Microfluidic mixers for studying protein folding.Journal of visualized experiments : JoVE · 2012Article
- Crowding effects on the small, fast-folding protein lambda6-85.Faraday discussions · 2012Article
- The fast and the slow: folding and trapping of λ6-85.Journal of the American Chemical Society · 2011Article
- Visualizing a one-way protein encounter complex by ultrafast single-molecule mixing.Nature methods · 2011Article
- Atomistic folding simulations of the five-helix bundle protein λ(6−85).Journal of the American Chemical Society · 2011Article
- The folding of single domain proteins--have we reached a consensus?Current opinion in structural biology · 2011Review
- A survey of lambda repressor fragments from two-state to downhill folding.Journal of molecular biology · 2010Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The protein lambda(6-85) has been implicated in barrierless folding by observations of kinetic relaxation after nanosecond T-jump. In this work we observed folding of this protein after dilution of a high denaturant in an ultrarapid microfluidic mixer at temperatures far below the thermal midpoint. The observations of total intensity and spectral shift of tryptophan fluorescence yielded distinctly different kinetics and activation energies. These results may be explained as diffusion on a low-barrier, one-dimensional, free-energy surface, with different probes having different sensitivities along the reaction coordinate. Additionally, we observed an extremely fast phase within the mixing time that was not observed by T-jump, suggesting that the ensemble of unfolded states populated at high denaturant is distinct from those accessible at high temperature.
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Registered trials
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.