ReviewBiomolecules2020
Solution of Levinthal's Paradox and a Physical Theory of Protein Folding Times.
Review in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed.
- Improving the Reliability of Protein Folding Rate Predictions by Applying Guidelines for Validating QSAR/QSPR Models.International journal of molecular sciences · 2026Article
- Factors controlling protein evolvability-at the molecular scale.European biophysics journal : EBJ · 2026Article
- Bridging Scales: Coarse-Grained Protein Models in Computational Biology.Advances in experimental medicine and biology · 2026Review
- The role of molecular chaperone CCT/TRiC in translation elongation: A literature review.Heliyon · 2024Review
- Base Pairing Promoted the Self-Organization of Genetic Coding, Catalysis, and Free-Energy Transduction.Life (Basel, Switzerland) · 2024Review
- Biophysical Evidence for the Amyloid Formation of a Recombinant Rab2 Isoform ofProtein and peptide letters · 2024Article
- Revolutionizing Medicinal Chemistry: The Application of Artificial Intelligence (AI) in Early Drug Discovery.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Protein folding rate evolution upon mutations.Biophysical reviews · 2023Review
- Protein folding problem: enigma, paradox, solution.Biophysical reviews · 2022Review
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- DMSO-Quenched H/D-Exchange 2D NMR Spectroscopy and Its Applications in Protein Science.Molecules (Basel, Switzerland) · 2022Review
- Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative Diseases.International journal of molecular sciences · 2022Review
- Review
- Life in Phases: Intra- and Inter- Molecular Phase Transitions in Protein Solutions.Biomolecules · 2019Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
"How do proteins fold?" Researchers have been studying different aspects of this question for more than 50 years. The most conceptual aspect of the problem is how protein can find the global free energy minimum in a biologically reasonable time, without exhaustive enumeration of all possible conformations, the so-called "Levinthal's paradox." Less conceptual but still critical are aspects about factors defining folding times of particular proteins and about perspectives of machine learning for their prediction. We will discuss in this review the key ideas and discoveries leading to the current understanding of folding kinetics, including the solution of Levinthal's paradox, as well as the current state of the art in the prediction of protein folding times.
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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.