ArticleProtein science : a publication of the Protein Society2006
Solvent-tuning the collapse and helix formation time scales of lambda(6-85)*.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 31 citations in OpenAlex.
- How cooperative are protein folding and unfolding transitions?Protein science : a publication of the Protein Society · 2016Review
- 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
- Misplaced helix slows down ultrafast pressure-jump protein folding.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
- Structural Characterization of λ-Repressor Folding from All-Atom Molecular Dynamics Simulations.The journal of physical chemistry letters · 2012Article
- Loop and stem dynamics during RNA hairpin folding and unfolding.RNA (New York, N.Y.) · 2010Article
- A survey of lambda repressor fragments from two-state to downhill folding.Journal of molecular biology · 2010Article
- Direct observation of downhill folding of lambda-repressor in a microfluidic mixer.Biophysical journal · 2009Article
- Slowing down downhill folding: a three-probe study.Biophysical journal · 2009Article
- Reaching the protein folding speed limit with large, sub-microsecond pressure jumps.Nature methods · 2009Article
- Analysis of the free-energy surface of proteins from reversible folding simulations.PLoS computational biology · 2009Article
- How general is the nucleation-condensation mechanism?Proteins · 2008Article
- Simulation-based fitting of protein-protein interaction potentials to SAXS experiments.Biophysical journal · 2008Article
- An experimental survey of the transition between two-state and downhill protein folding scenarios.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- An extended dynamical hydration shell around proteins.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Structural study of hNck2 SH3 domain protein in solution by circular dichroism and X-ray solution scattering.Biophysical chemistryArticle
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The lambda(6-85)(*) pseudo-wild type of lambda repressor fragment is a fast two-state folder (k(f) approximately 35 microsec(-1) at 58 degrees C). Previously, highly stable lambda(6-85)(*) mutants with k(f) > 30 microsec(-1) have been engineered to fold nearly or fully downhill. Stabilization of the native state by solvent tuning might also tune lambda(6-85)(*) away from two-state folding. We test this prediction by examining the folding thermodynamics and kinetics of lambda(6-85)(*) in a stabilizing solvent, 45% by weight aqueous ethylene glycol at -28 degrees C. Detection of kinetics by circular dichroism at 222 nm (sensitive to helix content) and small angle X-ray scattering (measuring the radius of gyration) shows that refolding from guanidine hydrochloride denatured conditions exhibits very different time scales for collapse and secondary structure formation: the two processes become decoupled. Collapse remains a low-barrier activated process, while the fastest of several secondary structure formation time scales approaches the downhill folding limit. Two-state folding of lambda(6-85)(*) is not a robust process.
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