ArticleBiophysical journal2003
Proline can have opposite effects on fast and slow protein folding phases.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 49 citations in OpenAlex.
- Force writes memory: proline isomerization as a molecular memory switch.Biochemical Society transactions · 2025Review
- Genetic Basis of Hypertrophic Cardiomyopathy in Cats.Current issues in molecular biology · 2024Review
- Electron videography of a lipid-protein tango.Science advances · 2024Article
- Replacement of the native cis prolines by alanine leads to simplification of the complex folding mechanism of a small globular protein.Biophysical journal · 2023Article
- Scaffold Hopping Transformations Using Auxiliary Restraints for Calculating Accurate Relative Binding Free Energies.Journal of chemical theory and computation · 2021Article
- An APP ectodomain mutation outside of the Aβ domain promotes Aβ production in vitro and deposition in vivo.The Journal of experimental medicine · 2021Article
- Entropic Control of an Excited Folded-Like Conformation in a Disordered Protein Ensemble.Journal of molecular biology · 2018Article
- Propensity for cis-Proline Formation in Unfolded Proteins.Chembiochem : a European journal of chemical biology · 2018Article
- Hydrogen bonds are a primary driving force for de novo protein folding.Acta crystallographica. Section D, Structural biology · 2017Article
- Novel polysaccharide binding to the N-terminal tail of galectin-3 is likely modulated by proline isomerization.Glycobiology · 2017Article
- Dodine as a transparent protein denaturant for circular dichroism and infrared studies.Protein science : a publication of the Protein Society · 2016Article
- 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
- Thermally denatured state determines refolding in lipase: mutational analysis.Protein science : a publication of the Protein Society · 2009Article
- Role of a pro-sequence in the secretory pathway of prothyrotropin-releasing hormone.The Journal of biological chemistry · 2008Article
- Asymmetric effect of domain interactions on the kinetics of folding in yeast phosphoglycerate kinase.Protein science : a publication of the Protein Society · 2005Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proline isomerization is well known to cause additional slow phases during protein refolding. We address a new question: does the presence of prolines significantly affect the very fast kinetics that lead to the formation of folding intermediates? We examined both the very slow (10-100 min) and very fast (4 micro s-2.5 ms) folding kinetics of the two-domain enzyme yeast phosphoglycerate kinase by temperature-jump relaxation. Phosphoglycerate kinase contains a conserved cis-proline in position 204, in addition to several trans-prolines. Native cis-prolines have the largest effect on folding kinetics because the unfolded state favors trans isomerization, so we compared the kinetics of a P204H mutant with the wild-type as a proof of principle. The presence of Pro-204 causes an additional slow phase upon refolding from the cold denatured state, as reported in the literature. Contrary to this, the fast folding events are sped up in the presence of the cis-proline, probably by restriction of the conformational space accessible to the molecule. The wild-type and Pro204His mutant would be excellent models for off-lattice simulations probing the effects of conformational restriction on short timescales.
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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.