ReviewCurrent opinion in structural biology2012
How, when and why proteins collapse: the relation to folding.
Review in Current opinion in structural biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
What it found
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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
59 citing papers in PubMed.
- Interlayer rotation (twisting) switches interlayer mobility in moiré superlattices.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Accuracy of distance distributions and dynamics from single-molecule FRET.Biophysical journal · 2025Article
- Identifying Sequence Effects on Chain Dimensions of Disordered Proteins by Integrating Experiments and Simulations.JACS Au · 2024Article
- Amino Acid Residue-Specific Ramachandran Distributions Derived from a Simple Mean Field Potential.ACS physical chemistry Au · 2024Article
- Probe capsid structure stability and dynamics of adeno-associated virus as an important viral vector for gene therapy by hydrogen-deuterium exchange-mass spectrometry.Protein science : a publication of the Protein Society · 2024Article
- Methotrexate for Drug Repurposing as an Anti-Aggregatory Agent to Mercuric Treated α-Chymotrypsinogen-A.The protein journal · 2024Article
- Structure of Single-Chain Nanoparticles under Crowding Conditions: A Random Phase Approximation Approach.Macromolecules · 2023Article
- Replacement of the native cis prolines by alanine leads to simplification of the complex folding mechanism of a small globular protein.Biophysical journal · 2023Article
- Article
- The Protein Unfolded State: One, No One and One Hundred Thousand.Journal of the American Chemical Society · 2022Review
- Linking Gas-Phase and Solution-Phase Protein Unfolding via Mobile Proton Simulations.Analytical chemistry · 2022Article
- Protein chain collapse modulation and folding stimulation by GroEL-ES.Science advances · 2022Article
- Saturation Mutagenesis of the Transmembrane Region of HokC inInternational journal of molecular sciences · 2021Article
- Article
- Thermal inactivation scaling applied for SARS-CoV-2.Biophysical journal · 2021Article
- Thermosensitive Hydration of Four Acrylamide-Based Polymers in Coil and Globule Conformations.The journal of physical chemistry. B · 2020Article
- The Last Secret of Protein Folding: The Real Relationship Between Long-Range Interactions and Local Structures.The protein journal · 2020Review
- Dramatic Shape Changes Occur as CytochromeThe journal of physical chemistry. B · 2020Article
- Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway.Cells · 2020Review
- Friction-Limited Folding of Disulfide-Reduced Monomeric SOD1.Biophysical journal · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
Abstract
Unfolded proteins under strongly denaturing conditions are highly expanded. However, when the conditions are more close to native, an unfolded protein may collapse to a compact globular structure distinct from the folded state. This transition is akin to the coil-globule transition of homopolymers. Single-molecule FRET experiments have been particularly conducive in revealing the collapsed state under conditions of coexistence with the folded state. The collapse can be even more readily observed in natively unfolded proteins. Time-resolved studies, using FRET and small-angle scattering, have shown that the collapse transition is a very fast event, probably occurring on the submicrosecond time scale. The forces driving collapse are likely to involve both hydrophobic and backbone interactions. The loss of configurational entropy during collapse makes the unfolded state less stable compared to the folded state, thus facilitating folding.
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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.