The hydrophobic effect and the organization of living matter.

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.

[1]  R. Henderson,et al.  Three-dimensional model of purple membrane obtained by electron microscopy , 1975, Nature.

[2]  P. Strittmatter,et al.  A form of cytochrome b5 that contains an additional hydrophobic sequence of 40 amino acid residues. , 1971, Proceedings of the National Academy of Sciences of the United States of America.

[3]  D. E. Green.  MEMBRANE PROTEINS: A PERSPECTIVE , 1972, Annals of the New York Academy of Sciences.

[4]  Charles Tanford,et al.  Theory of micelle formation in aqueous solutions , 1974 .

[5]  E. Korn,et al.  Single bilayer liposomes prepared without sonication. , 1973, Biochimica et biophysica acta.

[6]  S. Singer,et al.  The Fluid Mosaic Model of the Structure of Cell Membranes , 1972, Science.

[7]  Henry S. Frank,et al.  Free Volume and Entropy in Condensed Systems III. Entropy in Binary Liquid Mixtures; Partial Molal Entropy in Dilute Solutions; Structure and Thermodynamics in Aqueous Electrolytes , 1945 .

[8]  C. Tanford,et al.  The two-domain structure of cytochrome b5 in deoxycholate solution. , 1975, Biochemistry.

[9]  C. Tanford,et al.  Hydrophobicity of Long Chain n-Alkyl Carboxylic Acids, as Measured by Their Distribution Between Heptane and Aqueous Solutions. , 1973, Proceedings of the National Academy of Sciences of the United States of America.

[10]  C. Anfinsen.  Principles that govern the folding of protein chains. , 1973, Science.

[11]  C. Tanford,et al.  Characterization of membrane proteins in detergent solutions. , 1976, Biochimica et biophysica acta.

[12]  Ching-Hsien Huang,et al.  Phosphatidylcholine vesicles. Formation and physical characteristics , 1969 .

[13]  T. Higuchi,et al.  Thermodynamic group contributions from ion pair extraction equilibriums for use in the prediction of partition coefficients. Correlation of surface area with group contributions , 1973 .

[14]  Robert B. Hermann,et al.  Theory of hydrophobic bonding. II. Correlation of hydrocarbon solubility in water with solvent cavity surface area , 1972 .

[15]  C. Tanford,et al.  Cholesterol in aqueous solution: hydrophobicity and self-association. , 1975, Biochemistry.

[16]  V. Braun,et al.  Covalent lipoprotein from the outer membrane of Escherichia coli. , 1975, Biochimica et biophysica acta.

[17]  M. Levitt,et al.  Computer simulation of protein folding , 1975, Nature.

[18]  E. Dennis,et al.  A carbon-13 and proton nuclear magnetic resonance study on the structure and mobility of nonionic alkyl polyoxyethylene ether micelles , 1977 .

[19]  W. Kauzmann.  Some factors in the interpretation of protein denaturation. , 1959, Advances in protein chemistry.

[20]  C. A. Lewis,et al.  A vapor phase analysis of the hydrophobic effect. , 1976, Journal of theoretical biology.

[21]  C. Chothia.  Structural invariants in protein folding , 1975, Nature.

[22]  C. Tanford,et al.  Empirical correlation between hydrophobic free energy and aqueous cavity surface area. , 1974, Proceedings of the National Academy of Sciences of the United States of America.

[23]  C. Tanford,et al.  Size and shape of globular micelles formed in aqueous solution by n-alkyl polyoxyethylene ethers , 1977 .

[24]  L. Packer,et al.  The structural role of lipids in mitochondrial and sarcoplasmic reticulum membranes. Freeze-fracture electron microscopy studies. , 1974, Biochimica et biophysica acta.

[25]  M. Inouye.  A three-dimensional molecular assembly model of a lipoprotein from the Escherichia coli outer membrane. , 1974, Proceedings of the National Academy of Sciences of the United States of America.

[26]  H. Hauser,et al.  Single bilayer vesicles prepared without sonication. Physico-chemical properties. , 1976, Biochimica et biophysica acta.

[27]  W. Konigsberg,et al.  Reinvestigation of a region of the fd bacteriophage coat protein sequence. , 1974, Journal of molecular biology.

[28]  E. Dennis,et al.  The size, shape, and hydration of nonionic surfactant micelles. Triton X-100 , 1977 .

[29]  C. McAuliffe,et al.  Solubility in Water of Paraffin, Cycloparaffin, Olefin, Acetylene, Cycloolefin, and Aromatic Hydrocarbons1 , 1966 .