ArticleProtein science : a publication of the Protein Society2005
Asymmetric effect of domain interactions on the kinetics of folding in yeast phosphoglycerate kinase.
Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 35 citations in OpenAlex.
- Features of Protein Unfolding Transitions and Their Relation to Domain Topology Probed by Single-Molecule FRET.Biomolecules · 2023Article
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- Review
- Investigating the trade-off between folding and function in a multidomain Y-family DNA polymerase.eLife · 2020Article
- Mapping Multiple Distances in a Multidomain Protein for the Identification of Folding Intermediates.Biophysical journal · 2020Article
- Unraveling the Mechanical Unfolding Pathways of a Multidomain Protein: Phosphoglycerate Kinase.Biophysical journal · 2018Article
- On-chip measurements of protein unfolding from direct observations of micron-scale diffusion.Chemical science · 2018Article
- Same but not alike: Structure, flexibility and energetics of domains in multi-domain proteins are influenced by the presence of other domains.PLoS computational biology · 2018Article
- Identification of cancer fusion drivers using network fusion centrality.Bioinformatics (Oxford, England) · 2013Article
- Role of domain interactions in the collective motion of phosphoglycerate kinase.Biophysical journal · 2013Article
- Comparing the folding and misfolding energy landscapes of phosphoglycerate kinase.Biophysical journal · 2012Article
- Protein stability and folding kinetics in the nucleus and endoplasmic reticulum of eucaryotic cells.Biophysical journal · 2011Article
- What lessons can be learned from studying the folding of homologous proteins?Methods (San Diego, Calif.) · 2010Review
- Studying the folding of multidomain proteins.HFSP journal · 2008Article
- Predicting protein folding pathways at the mesoscopic level based on native interactions between secondary structure elements.BMC bioinformatics · 2008Article
- The folding pathway of a single domain in a multidomain protein is not affected by its neighbouring domain.Journal of molecular biology · 2008Article
- Distinguishing specific and nonspecific interdomain interactions in multidomain proteins.Biophysical journal · 2008Article
- The influence of interdomain interactions on the intradomain motions in yeast phosphoglycerate kinase: a molecular dynamics study.Biophysical journal · 2007Article
- Apparent cooperativity in the folding of multidomain proteins depends on the relative rates of folding of the constituent domains.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aim of this work is to shed more light on the effect of domain-domain interactions on the kinetics and the pathway of protein folding. A model protein system consisting of several single-tryptophan variants of the two-domain yeast phosphoglycerate kinase (PGK) and its individual domains was studied. Refolding was initiated from the guanidine-unfolded state by stopped-flow or manual mixing and monitored by tryptophan fluorescence from 1 msec to 1000 sec. Denaturant titrations of both individual domains showed apparent two-state unfolding transitions. Refolding kinetics of the individual domains from different denaturant concentrations, however, revealed the presence of intermediate structures during titration for both domains. Refolding of the same domains within the complete protein showed that domain-domain interactions direct the folding of both domains, but in an asymmetric way. Folding of the N domain was already altered within 1 msec, while detectable changes in the folding of the C domain occurred only 60-100 msec after initiating refolding. All mutants showed a hyperfluorescent kinetic intermediate. Both the disappearance of this intermediate and the completion of the folding were significantly faster in the individual N domain than in the complete protein. On the contrary, folding of the individual C domain was slower than in the complete protein. The presence of the C domain directs the refolding of the N domain along a completely different pathway than that of the individual N domain, while folding of the individual C domain follows the same path as within the complete protein.
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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.