ArticleProceedings of the National Academy of Sciences of the United States of America2007
Predicting coupling limits from an experimentally determined energy landscape.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed.
- Large Ankyrin repeat proteins are formed with similar and energetically favorable units.PloS one · 2020Article
- Decoupling a tandem-repeat protein: Impact of multiple loop insertions on a modular scaffold.Scientific reports · 2019Article
- Folding cooperativity and allosteric function in the tandem-repeat protein class.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- High-Resolution Mapping of a Repeat Protein Folding Free Energy Landscape.Biophysical journal · 2016Article
- How to Build a Complex, Functional Propeller Protein, From Parts.Trends in biochemical sciences · 2016Article
- A disorder-induced domino-like destabilization mechanism governs the folding and functional dynamics of the repeat protein IκBα.PLoS computational biology · 2013Article
- Modulation of folding kinetics of repeat proteins: interplay between intra- and interdomain interactions.Biophysical journal · 2012Article
- Unique features of the folding landscape of a repeat protein revealed by pressure perturbation.Biophysical journal · 2010Article
- The HD-exchange motions of ribosomal protein S6 are insensitive to reversal of the protein-folding pathway.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- C-terminal deletion of leucine-rich repeats from YopM reveals a heterogeneous distribution of stability in a cooperatively folded protein.Protein science : a publication of the Protein Society · 2009Article
- What have we learned from the studies of two-state folders, and what are the unanswered questions about two-state protein folding?Physical biology · 2009Article
- Predicting repeat protein folding kinetics from an experimentally determined folding energy landscape.Protein science : a publication of the Protein Society · 2009Article
- Thermodynamics, kinetics, and salt dependence of folding of YopM, a large leucine-rich repeat protein.Journal of molecular biology · 2008Article
- Mapping the energy landscape of repeat proteins using NMR-detected hydrogen exchange.Journal of molecular biology · 2008Article
- The energy landscapes of repeat-containing proteins: topology, cooperativity, and the folding funnels of one-dimensional architectures.PLoS computational biology · 2008Article
- Structural insights into an equilibrium folding intermediate of an archaeal ankyrin repeat protein.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Folding landscapes of ankyrin repeat proteins: experiments meet theory.Current opinion in structural biology · 2008Review
- Repeat-protein folding: new insights into origins of cooperativity, stability, and topology.Archives of biochemistry and biophysics · 2008Review
- The protein folding problem.Annual review of biophysics · 2008Review
- The plastic landscape of repeat proteins.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Repeat proteins are composed of tandem structural modules in which close contacts do not extend beyond adjacent repeats. Despite the local nature of these close contacts, repeat proteins often unfold as a single, highly coupled unit. Previous studies on the Notch ankyrin domain suggest that this lack of equilibrium unfolding intermediates results both from stabilizing interfaces between each repeat and from a roughly uniform distribution of stability across the folding energy landscape. To investigate this idea, we have generated 15 variants of the Notch ankyrin domain with single and multiple destabilizing substitutions that make the energy landscape uneven. By applying a free energy additivity analysis to these variants, we quantified the destabilization threshold over which repeats 6 and 7 decouple from repeats 1-5. The free energy coupling limit suggested by this additivity analysis ( approximately 4 kcal/mol) is also reflected in m-value analysis and in differences among equilibrium unfolding transitions as monitored by CD versus fluorescence for all 15 variants. All of these observations are quantitatively predicted by analyzing the response of the experimentally determined energy landscape to increasing unevenness. These results highlight the importance of a uniform distribution of local stability in achieving cooperative unfolding.
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.