ReviewThe Biochemical journal2016
When fast is better: protein folding fundamentals and mechanisms from ultrafast approaches.
Review in The Biochemical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- NMR evidence for residue-based LFER relationship in two-state folding-unfolding equilibrium of the spectrin SH3 domain in acidic solutions.Biophysics and physicobiology · 2026Article
- You must be flexible enough to be trained, Mr. Dynamics simulator.Molecular diversity · 2024Article
- Reviewing the Structure-Function Paradigm in Polyglutamine Disorders: A Synergistic Perspective on Theoretical and Experimental Approaches.International journal of molecular sciences · 2024Review
- Hydrogen bonding heterogeneity correlates with protein folding transition state passage time as revealed by data sonification.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Protein conformational ensembles in function: roles and mechanisms.RSC chemical biology · 2023Review
- Einstein Model of a Graph to Characterize Protein Folded/Unfolded States.Molecules (Basel, Switzerland) · 2023Article
- Protein folding rate evolution upon mutations.Biophysical reviews · 2023Review
- Residue-based correlation between equilibrium and rate constants is an experimental formulation of the consistency principle for smooth structural changes of proteins.Biophysics and physicobiology · 2023Article
- Enhanced statistical sampling reveals microscopic complexity in the talin mechanosensor folding energy landscape.Nature physics · 2023Article
- Evolutionary adaptation of the protein folding pathway for secretability.The EMBO journal · 2022Article
- A protocol to measure slow protein dynamics of the cholera toxin B pentamers using broadband dielectric spectroscopy.STAR protocols · 2022Article
- Article
- Mutational Analysis of Protein Folding Transition States: Phi Values.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Labeling of Proteins for Single-Molecule Fluorescence Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2022Article
- In Silico Modeling of the Influence of Environment on Amyloid Folding Using FOD-M Model.International journal of molecular sciences · 2021Article
- Thermally-Induced Shape-Memory Behavior of Degradable Gelatin-Based Networks.International journal of molecular sciences · 2021Article
- Unfolding bovine α-lactalbumin with T-jump: Characterizing disordered intermediates via time-resolved x-ray solution scattering and molecular dynamics simulations.The Journal of chemical physics · 2021Article
- Druggable Transient Pockets in Protein Kinases.Molecules (Basel, Switzerland) · 2021Review
- Mapping Function from Dynamics: Future Challenges for Network-Based Models of Protein Structures.Frontiers in molecular biosciences · 2021Article
- Quantitative comparison between sub-millisecond time resolution single-molecule FRET measurements and 10-second molecular simulations of a biosensor protein.PLoS computational biology · 2020Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Protein folding research stalled for decades because conventional experiments indicated that proteins fold slowly and in single strokes, whereas theory predicted a complex interplay between dynamics and energetics resulting in myriad microscopic pathways. Ultrafast kinetic methods turned the field upside down by providing the means to probe fundamental aspects of folding, test theoretical predictions and benchmark simulations. Accordingly, experimentalists could measure the timescales for all relevant folding motions, determine the folding speed limit and confirm that folding barriers are entropic bottlenecks. Moreover, a catalogue of proteins that fold extremely fast (microseconds) could be identified. Such fast-folding proteins cross shallow free energy barriers or fold downhill, and thus unfold with minimal co-operativity (gradually). A new generation of thermodynamic methods has exploited this property to map folding landscapes, interaction networks and mechanisms at nearly atomic resolution. In parallel, modern molecular dynamics simulations have finally reached the timescales required to watch fast-folding proteins fold and unfold in silico All of these findings have buttressed the fundamentals of protein folding predicted by theory, and are now offering the first glimpses at the underlying mechanisms. Fast folding appears to also have functional implications as recent results connect downhill folding with intrinsically disordered proteins, their complex binding modes and ability to moonlight. These connections suggest that the coupling between downhill (un)folding and binding enables such protein domains to operate analogically as conformational rheostats.
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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.