ArticleNature chemical biology2013
Cold denaturation of a protein dimer monitored at atomic resolution.
Article in Nature chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Effects of Hydration on Transthyretin Conformational Dynamics and Oligomerization.Biochemistry · 2025Article
- Water Plays Key Roles in Stabilities of Wild Type and Mutant Transthyretin Complexes.Journal of the American Society for Mass Spectrometry · 2024Article
- Cascade autohydrolysis of Alzheimer's Aβ peptides.Chemical science · 2023Article
- Reversible switching between two common protein folds in a designed system using only temperature.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Interdiction in the Early Folding of the p53 DNA-Binding Domain Leads to Its Amyloid-Like Misfolding.Molecules (Basel, Switzerland) · 2022Article
- From Protein Design to the Energy Landscape of a Cold Unfolding Protein.The journal of physical chemistry. B · 2022Article
- Functional and Regulatory Roles of Fold-Switching Proteins.Structure (London, England : 1993) · 2021Review
- The near-symmetry of protein oligomers: NMR-derived structures.Scientific reports · 2020Article
- Hydration shell differentiates folded and disordered states of a Trp-cage miniprotein, allowing characterization of structural heterogeneity by wide-line NMR measurements.Scientific reports · 2019Article
- Dual-Family Peptidylprolyl Isomerases (Immunophilins) of Select Monocellular Organisms.Biomolecules · 2018Review
- Structural accommodations accompanying splicing of a group II intron RNP.Nucleic acids research · 2018Article
- Identification and Characterization of an Inside-Out Folding Intermediate of T4 Phage Sliding Clamp.Biophysical journal · 2017Article
- Water Determines the Structure and Dynamics of Proteins.Chemical reviews · 2016Review
- The Complex Energy Landscape of the Protein IscU.Biophysical journal · 2015Article
- "Invisible" conformers of an antifungal disulfide protein revealed by constrained cold and heat unfolding, CEST-NMR experiments, and molecular dynamics calculations.Chemistry (Weinheim an der Bergstrasse, Germany) · 2015Article
- γS-crystallin proteins from the Antarctic nototheniid toothfish: a model system for investigating differential resistance to chemical and thermal denaturation.The journal of physical chemistry. B · 2014Article
- Structural biology: Protein self-assembly intermediates.Nature chemical biology · 2013Article
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8 authors.
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Abstract
Protein folding and unfolding are crucial for a range of biological phenomena and human diseases. Defining the structural properties of the involved transient species is therefore of prime interest. Using a combination of cold denaturation with NMR spectroscopy, we reveal detailed insight into the unfolding of the homodimeric repressor protein CylR2. Seven three-dimensional structures of CylR2 at temperatures from 25 °C to -16 °C reveal a progressive dissociation of the dimeric protein into a native-like monomeric intermediate followed by transition into a highly dynamic, partially folded state. The core of the partially folded state seems critical for biological function and misfolding.
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