ArticleProtein science : a publication of the Protein Society2011
The Levinthal paradox of the interactome.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Selection for Molecularly Complementary Modules (MCMs) Drives the Origins and Evolution of Pleiofunctional, Epistatic Interactomes (PEIs).Life (Basel, Switzerland) · 2026Review
- Multiparameter screen optimizes immunoprecipitation.BioTechniques · 2024Article
- Networks of Networks: An Essay on Multi-Level Biological Organization.Frontiers in genetics · 2021Review
- Affinity proteomic dissection of the human nuclear cap-binding complex interactome.Nucleic acids research · 2020Article
- Modeling the assembly order of multimeric heteroprotein complexes.PLoS computational biology · 2018Article
- Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water.Science (New York, N.Y.) · 2017Article
- Searching for the Pareto frontier in multi-objective protein design.Biophysical reviews · 2017Review
- Article
- Misfolded proteins: from little villains to little helpers in the fight against cancer.Frontiers in oncology · 2015Review
- Licensing and due process in the turnover of bacterial RNA.RNA biology · 2013Review
- Cellular crowding imposes global constraints on the chemistry and evolution of proteomes.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Hydrogel formation by multivalent IDPs: A reincarnation of the microtrabecular lattice?Intrinsically disordered proteinsReview
Corrections and comments
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Authors and funding
2 authors.
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Abstract
The central biological question of the 21st century is: how does a viable cell emerge from the bewildering combinatorial complexity of its molecular components? Here, we estimate the combinatorics of self-assembling the protein constituents of a yeast cell, a number so vast that the functional interactome could only have emerged by iterative hierarchic assembly of its component sub-assemblies. A protein can undergo both reversible denaturation and hierarchic self-assembly spontaneously, but a functioning interactome must expend energy to achieve viability. Consequently, it is implausible that a completely "denatured" cell could be reversibly renatured spontaneously, like a protein. Instead, new cells are generated by the division of pre-existing cells, an unbroken chain of renewal tracking back through contingent conditions and evolving responses to the origin of life on the prebiotic earth. We surmise that this non-deterministic temporal continuum could not be reconstructed de novo under present conditions.
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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.