ReviewAnnual review of biophysics2008
The protein folding problem.
Review in Annual review of biophysics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 382 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
382 citing papers in PubMed.
- Evaluating AlphaFold Tools and Related Scoring Functions for Protein-peptide Complex Prediction.Genomics, proteomics & bioinformatics · 2026Article
- How proteins fold.Nature reviews. Molecular cell biology · 2026Article
- A Simulation-Free Topological Basis for Building Compact Koopman Models of Protein Folding.Journal of chemical information and modeling · 2026Article
- A Quantum-Classical Analysis of Variability in Peptide Energies and Conformations.The protein journal · 2026Article
- Condensates and cell states: A new paradigm for understanding tumor biology.Biophysical journal · 2026Review
- Methods for the establishment of enzymatic mechanisms - from QM to ML.Chemical science · 2026Review
- Coupled Binding and Folding of NS2B/NS3 Protease and Linker Effects Revealed by Topology-Based Modeling.The journal of physical chemistry. B · 2026Article
- Entropy quantum computing for fixed-backbone protein design.Scientific reports · 2026Article
- Article
- amyloid-predict and LLPS-predict: Predicting phase separation propensities in the intrinsically disordered proteome.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Bridging structure and function: artificial intelligence-based modelling of kidney proteins.Nature reviews. Nephrology · 2026Review
- Modifying recombinant purple acid phosphatase using computational design.European biophysics journal : EBJ · 2026Article
- Backbone double-mutant cycle analysis quantifies hydrogen-bond energies in proteins.Protein science : a publication of the Protein Society · 2026Article
- Coupled Binding and Folding of NS2B/NS3 Protease and Linker Effects Revealed by Topology-based Modeling.bioRxiv : the preprint server for biology · 2026Article
- A quantum-mechanical framework for million-atom scale biological systems.Communications chemistry · 2026Article
- How Does Genetic Information Enable Life?Bulletin of mathematical biology · 2026Article
- Amino acid composition drives aggregation during peptide synthesis.Nature chemistry · 2026Article
- Polymorphism in Self-Assembly of Short Peptoid Sequences.Polymer science & technology (Washington, D.C.) · 2026Article
- Analytical Physicochemical and Functional Studies to Compare AryoTrust, a Follow-On Biologics, with the Originator Trastuzumab (Herceptin).Pharmaceutics · 2026Article
- Computational design of functional random heteropolymers through atomistic simulations.PloS one · 2026Article
322 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
The "protein folding problem" consists of three closely related puzzles: (a) What is the folding code? (b) What is the folding mechanism? (c) Can we predict the native structure of a protein from its amino acid sequence? Once regarded as a grand challenge, protein folding has seen great progress in recent years. Now, foldable proteins and nonbiological polymers are being designed routinely and moving toward successful applications. The structures of small proteins are now often well predicted by computer methods. And, there is now a testable explanation for how a protein can fold so quickly: A protein solves its large global optimization problem as a series of smaller local optimization problems, growing and assembling the native structure from peptide fragments, local structures first.
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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.