Proposed Knobs-Into-Holes Packing for Several Membrane Proteins

References

• Blake C. C. F., Mair G. A., North A. C. T., Phillips C. C., Sarma V. R. On the conformation of the hen egg-white lysozmes molecule. Proc. R. Soc. (Lond) 1967; B167: 365–377
   Google Scholar
• Blow D. M., Burktoft J. J., Hartley B. S. Role of a buried acid group in the mechanism of chymotrypsin. Nature (Lond) 1969; 221: 337–340
   PubMed Web of Science ®Google Scholar
• Braun V., Bosch V. Sequence of the murein-lipoprotein and the attachment site of the lipid. Eur. J. Biochem. 1972; 28: 51–69
   PubMedGoogle Scholar
• Braun V., Bosch V. Repetitive sequencing in the murein lipoprotein of the cell wall of Escherichia coli. Proc. Natl. Acad. Sci. USA 1972; 69: 970–974
   PubMed Web of Science ®Google Scholar
• Bretscher M. S. Major human erythrocyte glycoprotein spans the cell membrane. Nature [New Biol.] 1971; 231: 229–232
   PubMedGoogle Scholar
• Chothia C., Levitt M., Richardson D. Structure of proteins: packing of α-helices and pleated sheets. Proc. Natl. Acad. Sci. USA 1977; 74: 4130–4134
   PubMed Web of Science ®Google Scholar
• Chou P. Y., Fasman G. D. Conformational parameters for amino acids in helical β-sheet, and random coil regions calculated from proteins. Biochemistry 1974; 13: 211–221
   PubMed Web of Science ®Google Scholar
• Chou P. Y., Fasman G. D. Prediction of protein conformation. Biochemistry 1974; 13: 222–245
   PubMed Web of Science ®Google Scholar
• Crick F. H.C. The packing of α-helices: simple coiled-coils. Acta Crystallogr. 1953; 6: 689–692
   Web of Science ®Google Scholar
• Crick F. H. C., Watson J. D. Structure of small viruses. Nature (Lond) 1956; 177: 473–474
   PubMed Web of Science ®Google Scholar
• Dunker A. K. On the structure and action of membrane proteins. J. Supramol Struct. 1977; S1: 659
   Google Scholar
• Dunker A. K., Marvin D. A. A model for membrane transport through α-helical protein pores. J. Theor. Biol. 1978; 72: 9–16
   PubMed Web of Science ®Google Scholar
• Dunker A. K., Zaleske D. J. Stereochemical considerations for constructing α-helical protein bundles with particular application to membrane proteins. Biochem. J. 1977; 163: 45–57
   Google Scholar
• Dunker A. K., Marvin D. A., Zaleske D. J., Jones T. Proposed structure and function of protein in membrane. Biophys. J. 1976; 16: 102a
   Google Scholar
• Eigen M., DeMayer L. Self-dissociation and protonic charge transport in water and ice. Proc. R. Soc. (Lond) 1958; A247: 505–533
   Google Scholar
• Furthmayer H., Marchesi V. T. Subunit structure of human erythrocyte glycophorin A. Biochemistry 1976; 15: 1173–1144
   Google Scholar
• Green N. M., Flanagan M. T. The prediction of the conformation of membrane proteins from the sequence of amino acids. Biochem. J. 1976; 153: 729–732
   PubMed Web of Science ®Google Scholar
• Hante K., Braun V. Covalent binding of lipid to protein. Eur. J. Biochem. 1973; 34: 284–296
   Google Scholar
• Henderson R. The structures of the purple membrane of Halobacterium halobium: analysis of the x-ray diffraction pattern. J. Mol. Biol. 1975; 93: 123–128
   Google Scholar
• Henderson R., Unwin P. N.T. Three dimensional model of purple membrane obtained by electron microscopy. Nature (Lond) 1975; 257: 28–32
   PubMed Web of Science ®Google Scholar
• Inouye M. A three dimensional molecular assembly model of a lipoprotin from the Escherichia coli outer membrane. Proc. Natl. Acad. Sci. USA 1974; 71: 2396–2400
   PubMed Web of Science ®Google Scholar
• Lenard J., Singer S. J. Protein conformation in cell membrane preparations as studied by optical rotary dispersion and circular dichroism. Proc. Natl. Acad. Sci. USA 1966; 56: 1828–1835
   PubMed Web of Science ®Google Scholar
• Lewis P. N., Momany F. A., Scheraga H. A. Folding polypeptide chains in proteins: a proposed mechanism for folding. Proc. Natl. Acad. Sci. USA 1971; 68: 2293–2297
   PubMed Web of Science ®Google Scholar
• Lim V. I. Structural principles of the globular organization of protein chains: a stereochemical theory of globular protein secondary structure. J. Mol. Biol. 1974; 88: 857–872
   PubMed Web of Science ®Google Scholar
• Lim V. I. Algorithms for prediction of α-helical and β-structural regions in globular protein. J. Mol. Biol. 1974; 88: 873–894
   PubMed Web of Science ®Google Scholar
• Marton L. S. G., Garvon J. E. Subunit structure of the major human erythrocyte glycoprotein: depolymerization by heating ghosts with sodium dodecyl sulfate. Biochem. Biophys. Res. Commun. 1973; 53: 1457–1461
   Google Scholar
• Marvin D. A., Hohn B. Filamentous bacterial viruses. Bacteriol. Rev. 1969; 33: 172–206
   PubMedGoogle Scholar
• Marvin D. A., Wachtel E. J. Structure and assembly of filmentous bacterial viruses. Nature (Lond) 1975; 253: 19–23
   PubMed Web of Science ®Google Scholar
• Mitchell P. Reversible coupling of transport and chemical reactions. Membranes and Ion Transport, E. E. Bittar. Wiley, New York 1970; Vol. 1: 192–256
   Google Scholar
• Morowitz H. J. Proton semiconductors and energy transduction in biological systems. Adv. Biol. Med. Phys. 1977; 17, (in press)
   Google Scholar
• Neville D. M. Circular dichroism of liver cell membrane organ specific protein. Biochem. Biophys. Res. Commun. 1969; 34: 60–63
   Google Scholar
• Onsager L. Thermodynamics and some molecular aspects of biology. The Neurosciences, G. L. Quarton, T. Melnechuk, F. O. Schmitt. Rockefeller University Press, New York 1967; 75–78
   Google Scholar
• Onsager L. Nobel Lecture: The Motion of Ions: Principles and Concepts. Nobel Foundation, Stockholm 1968
   Google Scholar
• Onsager L. Physics and Chemistry of Ice, E. Whalley. Royal Society Canada. 1973; 7–12
   Google Scholar
• Reeke G. N., Hartsuck J. A., Ludwig M. L., Quiocho F. A., Steitz T. A., Lipscomb W. N. The structure of carboxypeptidase A. VI. Some results of 2.0 Å resolution and the complex with glycol-tyrosine at 2.8 Å resolution. Proc. Natl. Acad. Sci. USA 1976; 58: 2220–2226
   Google Scholar
• Segrest J. P., Kahne I., Jackson R. L., Marchesi V. T. Major glycoprotein of the human erythrocyte membrane: evidence for an amphiphatic molecular structure. Arch. Biochem. Biophys. 1973; 155: 167–180
   PubMed Web of Science ®Google Scholar
• Shotton D. M., Watson J. C. Three dimensional structure of tosyl-elastase. Nature (Lond) 1970; 225: 811–816
   PubMed Web of Science ®Google Scholar
• Singer S. J. Structure and function of biological membranes. The Structure and Function of Biological Membranes, L. I. Rothfield. Academic Press, New York 1971; 145–122
   Google Scholar
• Steck T. L. The organization of proteins in the human red blood cell membranes. J. Cell Biol. 1974; 62: 1–19
   PubMed Web of Science ®Google Scholar
• Stein J. M., Fleischer S. Aggregation-induced red shift of the cotton effect of mitochrondrial structural protein. Proc. Natl. Acad. Sci. USA 1967; 58: 1292–1296
   Google Scholar
• Tuech J. K., Morrison M. Human erythrocyte membrane sialoglycoproteins: a study of interconversion. Biochem. Biophys. Res. Commun. 1974; 59: 352–358
   Google Scholar
• Unwin P. N. T., Henderson R. Molecular structure determination by electron microscopy of unsaturated crystalline specimens. J. Mol. Biol. 1975; 94: 425–440
   PubMed Web of Science ®Google Scholar
• Urry D. W., Mednieks M., Bejnarowicz E. Optical rotation of mitochrondrial membranes. Proc. Natl. Acad. Sci. USA 1967; 57: 1043–1047
   PubMed Web of Science ®Google Scholar
• Visser L., Robinson N. C., Tanford C. The two-domain structure of cytochrome b5 in deoxycholate solution. Biochemistry 1975; 14: 1194–1199
   PubMed Web of Science ®Google Scholar
• Wallach D. F. H., Gordon A. Lipid protein interactions in cellular membranes. Fed. Proc. 1968; 27: 1263–1268
   PubMedGoogle Scholar
• Wallach D. H. F., Winzler R. J. Evolving Strategies and Tactics in Membrane Research. Springer Verlag, New York 1974
   Google Scholar
• Wallach D. H. F., Zahler P. H. Protein conformations in cellular membranes. Proc. Natl. Acad. Sci. USA 1966; 56: 1552–1557
   PubMed Web of Science ®Google Scholar
• Walsh K. A., Neurath H. Trypsinogen and chymotrypsinogen as homologous proteins. Proc. Natl. Acad. Sci. USA 1964; 52: 884–889
   PubMed Web of Science ®Google Scholar
• Wang K., Richards F. M. An approach to nearest neighbor analysis of membrane proteins. J. Biol. Chem. 1974; 249: 8005–8023
   PubMed Web of Science ®Google Scholar
• Wright C. S., Alden R. A., Kraut J. A. Structure of subtilisin BPN' at 2.5 A resolution. Nature (Lond) 1969; 221: 235–242
   PubMedGoogle Scholar