ReviewBiochemistry2006
Dynamics, energetics, and structure in protein folding.
Review in Biochemistry, 2006. 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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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.
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Who cites it
32 citing papers in PubMed, 83 citations in OpenAlex.
- Early events in G-quadruplex folding captured by time-resolved small-angle X-ray scattering.Nucleic acids research · 2025Article
- Early Events in G-quadruplex Folding Captured by Time-Resolved Small-Angle X-Ray Scattering.bioRxiv : the preprint server for biology · 2024Article
- Identification of a novel risk factor for chronic wasting disease (CWD) in elk: S100G single nucleotide polymorphism (SNP) of the prion protein gene (PRNP).Veterinary research · 2023Article
- Predicting and Simulating Mutational Effects on Protein Folding Kinetics.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Structural insights and evaluation of the potential impact of missense variants on the interactions of SLIT2 with ROBO1/4 in cancer progression.Scientific reports · 2020Article
- New Insights into Folding, Misfolding, and Nonfolding Dynamics of a WW Domain.The journal of physical chemistry. B · 2020Article
- Understanding biochemical processes in the presence of sub-diffusive behavior of biomolecules in solution and living cells.Biophysical reviews · 2019Review
- Mapping Molecular Structure of Protein Locating on Nanoparticles with Limited Proteolysis.Analytical chemistry · 2019Article
- Instrumental Effects in the Dynamics of an Ultrafast Folding Protein under Mechanical Force.The journal of physical chemistry. B · 2018Article
- Microscopic nucleation and propagation rates of an alanine-based α-helix.Physical chemistry chemical physics : PCCP · 2017Article
- When fast is better: protein folding fundamentals and mechanisms from ultrafast approaches.The Biochemical journal · 2016Review
- A theoretical study of the unfolding pathway of reduced human serum albumin.Journal of molecular modeling · 2015Article
- Fast protein folding kinetics.Quarterly reviews of biophysics · 2014Review
- A molecular interpretation of 2D IR protein folding experiments with Markov state models.Biophysical journal · 2014Article
- Article
- The peptide-receptive transition state of MHC class I molecules: insight from structure and molecular dynamics.Journal of immunology (Baltimore, Md. : 1950) · 2012Article
- Equilibrium unfolding of the PDZ domain of β2-syntrophin.Biophysical journal · 2012Article
- The effect of electrostatics on the marginal cooperativity of an ultrafast folding protein.The Journal of biological chemistry · 2010Article
- Cyclic voltammetry: a new strategy for the evaluation of oxidative damage to bovine insulin.Protein science : a publication of the Protein Society · 2010Article
- Characterization of the cofactor-induced folding mechanism of a zinc-binding peptide using computationally designed mutants.Journal of molecular biology · 2009Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
For many decades, protein folding experimentalists have worked with no information about the time scales of relevant protein folding motions and without methods for estimating the height of folding barriers. Protein folding experiments have been interpreted using chemical models in which the folding process is characterized as a series of equilibria between two or more distinct states that interconvert with activated kinetics. Accordingly, the information to be extracted from experiments was circumscribed to apparent equilibrium constants and relative folding rates. Recent developments are changing this situation dramatically. The combination of fast-folding experiments with the development of analytical methods more closely connected to physical theory reveals that folding barriers in native conditions range from minimally high (approximately 14RT for the very slow folder AcP) to nonexistent. While slow-folding (i.e., > or = 1 ms) single-domain proteins are expected to fold in a two-state fashion, microsecond-folding proteins should exhibit complex behavior arising from crossing marginal or negligible folding barriers. This realization opens a realm of exciting opportunities for experimentalists. The free energy surface of a protein with a marginal (or no) barrier can be mapped using equilibrium experiments, which could resolve energetic factors from structural factors in folding. Kinetic experiments on these proteins provide the unique opportunity to measure folding dynamics directly. Furthermore, the complex distributions of time-dependent folding behaviors expected for these proteins might be accessible to single-molecule measurements. Here, we discuss some of these recent developments in protein folding, emphasizing aspects that can serve as a guide for experimentalists interested in exploiting this new avenue of research.
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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.