ArticleBiophysical journal2009
Slowing down downhill folding: a three-probe study.
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 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed.
- Chemical interactions modulate λProtein science : a publication of the Protein Society · 2023Article
- Threading single proteins through pores to compare their energy landscapes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Co-translational folding of α-helical proteins: structural studies of intermediate-length variants of the λ repressor.FEBS open bio · 2018Article
- 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
- CARPe diem.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
- Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Transient helical structure during PI3K and Fyn SH3 domain folding.The journal of physical chemistry. B · 2013Article
- Microsecond folding experiments and simulations: a match is made.Physical chemistry chemical physics : PCCP · 2013Article
- Integrative structural modeling with small angle X-ray scattering profiles.BMC structural biology · 2012Review
- A survey of lambda repressor fragments from two-state to downhill folding.Journal of molecular biology · 2010Article
- How to mark off paths on the protein energy landscape.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Structural study of hNck2 SH3 domain protein in solution by circular dichroism and X-ray solution scattering.Biophysical chemistryArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
The mutant Tyr22Trp/Glu33Tyr/Gly46Ala/Gly48Ala of lambda repressor fragment lambda(6-85) was previously assigned as an incipient downhill folder. We slow down its folding in a cryogenic water-ethylene-glycol solvent (-18 to -28 degrees C). The refolding kinetics are probed by small-angle x-ray scattering, circular dichroism, and fluorescence to measure the radius of gyration, the average secondary structure content, and the native packing around the single tryptophan residue. The main resolved kinetic phase of the mutant is probe independent and faster than the main phase observed for the pseudo-wild-type. Excess helical structure formed early on by the mutant may reduce the formation of turns and prevent the formation of compact misfolded states, speeding up the overall folding process. Extrapolation of our main cryogenic folding phase and previous T-jump measurements to 37 degrees C yields nearly the same refolding rate as extrapolated by Oas and co-workers from NMR line-shape data. Taken together, all the data consistently indicate a folding speed limit of approximately 4.5 micros for this fast folder.
Indexed as
Identifiers
What OpenQuestion holds
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.