The Hydrophobic Effect and the Organization of Living Matter
Abstract
Biological organization may be viewed as consisting of two stages: biosynthesis and assembly. The assembly process is largely under thermodynamic control; that is, as a first approximation it represents a search by each structural molecule for its state of lowest chemical potential. The hydrophobic effect is a unique organizing force, based on repulsion by the solvent instead of attractive forces at the site of organization. It is responsible for assembly of membranes of cells and intracellular compartments, and the absence of strong attractive forces makes the membranes fluid and deformable. The spontaneous folding of proteins, however, involves directed polar bonds, leading to more rigid structures. Intercellular organization probably involves polar bonds between cell surface proteins.
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In an example of a repertoire of NG = 100, composomes would appear only in micelles whose sizes are compatible with NMAX = 100.
“In an example of a repertoire of NG = 100, composomes would appear only in micelles, whose sizes are compatible with NMAX = 100 [90].”
From Systems protobiology: origin of life in lipid catalytic networks (2018) · cites this paper as [90]
Amphiphile mutual affinity is mostly due to hydrophobic tail-tail interactions and has relatively small dependence on the functional hydrophilic headgroup.
“This is because amphiphile mutual affinity is mostly due to the hydrophobic tail–tail interactions [90] and has relatively small dependence on the functional hydrophilic headgroup.”
From Systems protobiology: origin of life in lipid catalytic networks (2018) · cites this paper as [90]
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Segré, D., Ben-Eli, D., Deamer, D. W., & Lancet, D. (2001) · Origins of life and evolution of the biosphere · doi:10.1023/a:1006746807104 · Cited by 620 · see citing works
Compositional genomes: Prebiotic information transfer in mutually catalytic noncovalent assemblies
Segré, D., Ben-Eli, D., & Lancet, D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.8.4112 · Cited by 398 · see citing works
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Dobson, C. M., Ellison, G. B., Tuck, A. F., & Vaida, V. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.200366897 · Cited by 270 · see citing works
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Lancet, D., Zidovetzki, R., & Markovitch, O. (2018) · Journal of The Royal Society Interface · doi:10.1098/rsif.2018.0159 · Cited by 182 · see citing works
Kasianowicz, J., Benz, R., & McLaughlin, S. (1984) · The Journal of Membrane Biology · doi:10.1007/bf01868942 · Cited by 191 · see citing works
Segré, D., & Lancet, D. (2000) · The EMBO Reports · doi:10.1093/embo-reports/kvd063 · Cited by 133 · see citing works
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Kahana, A., Schmitt-Kopplin, P., & Lancet, D. (2019) · Astrobiology · doi:10.1089/ast.2019.2029 · Cited by 40 · see citing works
- Authors
- Tanford, C.
- Affiliations
- Duke Medical Center (US)
- Corresponding author
- Tanford, Charles
- Venue
- Science
- Published
- 1978-06-02
- Volume
- 200
- Issue
- 4345
- Pages
- 1012-1018
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2047115921
- Cited by
- 985
- References
- 0
- Citations by year
- 2026: 31 · 2025: 19 · 2024: 25 · 2023: 29 · 2022: 37 · 2021: 32 · 2020: 47 · 2019: 28 · 2018: 28 · 2017: 42 · 2016: 36 · 2015: 41 · 2014: 37 · 2013: 35 · 2012: 45
- FWCI
- 12.89
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Chemical and Physical Studies
- Keywords
- hydrophobic effect, biological organization, self-assembly, membrane assembly, intracellular compartments, membrane fluidity, protein folding, chemical potential, polar bonds, cell surface proteins, biosynthesis
- MeSH terms
- Cell Compartmentation, Cells, Chemistry, Physical, Membrane Proteins, Membranes, Micelles, Models, Biological, Phospholipids, Protein Conformation, Solubility, Thermodynamics, Water, Chemical Phenomena
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