ArticleNature structural & molecular biology2012
Visualizing transient protein-folding intermediates by tryptophan-scanning mutagenesis.
Article in Nature structural & molecular biology, 2012. 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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Who cites it
19 citing papers in PubMed, 60 citations in OpenAlex.
- Structure of a transient protein-folding intermediate by pressure-jump NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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- Chemoproteomics Identifies State-Dependent and Proteoform-Selective Caspase-2 Inhibitors.Journal of the American Chemical Society · 2024Article
- Human γS-Crystallin Resists Unfolding Despite Extensive Chemical Modification from Exposure to Ionizing Radiation.The journal of physical chemistry. B · 2022Article
- Monitoring protein conformational changes using fluorescent nanoantennas.Nature methods · 2022Article
- Inhibitor Mimetic Mutations in theACS chemical biology · 2021Article
- Tryptophan scanning mutagenesis as a way to mimic the compound-bound state and probe the selectivity of allosteric inhibitors in cells.Chemical science · 2020Article
- Heck Diversification of Indole-Based Substrates under Aqueous Conditions: From Indoles to Unprotected Halo-tryptophans and Halo-tryptophans in Natural Product Derivatives.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019Article
- Interrupted Pressure-Jump NMR Experiments Reveal Resonances of On-Pathway Protein Folding Intermediate.The journal of physical chemistry. B · 2018Article
- Conformational rearrangements of the C1 ring in KaiC measure the timing of assembly with KaiB.Scientific reports · 2018Article
- Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Observing a late folding intermediate of Ubiquitin at atomic resolution by NMR.Protein science : a publication of the Protein Society · 2016Article
- The effects of organic solvents on the folding pathway and associated thermodynamics of proteins: a microscopic view.Scientific reports · 2016Article
- Inside-out Ca(2+) signalling prompted by STIM1 conformational switch.Nature communications · 2015Article
- X-ray scattering experiments with high-flux X-ray source coupled rapid mixing microchannel device and their potential for high-flux neutron scattering investigations.The European physical journal. E, Soft matter · 2013Article
- Atomic-level description of ubiquitin folding.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Methionine mutations of outer membrane protein X influence structural stability and beta-barrel unfolding.PloS one · 2013Article
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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
To understand how proteins fold, assemble and function, it is necessary to characterize the structure and dynamics of each state they adopt during their lifetime. Experimental characterization of the transient states of proteins remains a major challenge because high-resolution structural techniques, including NMR and X-ray crystallography, cannot be directly applied to study short-lived protein states. To circumvent this limitation, we show that transient states during protein folding can be characterized by measuring the fluorescence of tryptophan residues, introduced at many solvent-exposed positions to determine whether each position is native-like, denatured-like or non-native-like in the intermediate state. We use this approach to characterize a late-folding-intermediate state of the small globular mammalian protein ubiquitin, and we show the presence of productive non-native interactions that suggest a 'flycatcher' mechanism of concerted binding and folding.
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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.