SEARCH

SEARCH BY CITATION

References

  • Allen, J.P., Feher, G., Yeates, T.O., Komiya, H., & Rees, D.C. (1987). Structure of the reaction center from Rhodobacter sphaeroides R-26: The protein subunits. Proc. Natl. Acad. Sci. USA 84, 61626166.
  • Allen, J.P., Feher, G., Yeates, T.O., Rees, D.C., Deisenhofer, J., Michel, H., & Huber, R. (1986). Structural homology of reaction centers from Rhodopseudomonas sphaeroides and Rhodopseudomonas viridis as determined by X-ray diffraction. Proc. Natl. Acad. Sci. USA 83, 85898593.
  • Appell, K.C. & Low, P.S. (1981). Partial structural characterization of cytoplasmic domain of the erythrocyte membrane protein, Band 3. J. Biol. Chem. 256, 1110411111.
  • Bolotina, I.A., Chekhov, V.O., Lugauskas, V.Y., & Ptitsyn, O.B. (1981). Determination of the secondary structure of proteins from circular dichroism spectra. III. Protein derived reference spectra for antiparallel and parallel β structures. Mol. Biol. 15, 130137. [Translated from Molekulyarnaya Biologiya (USSR) 15, 167–175 (1980).
  • Bovey, F.A. (1988). NMR of solids. In Nuclear Magnetic Resonance Spectroscopy, 2nd Ed. (Bovey, F.A., Jelinsky, L., & Mirau, P.A., Eds.), pp. 399436. Academic Press, New York.
  • Brahms, S. & Brahms, J. (1980). Determination of protein secondary structure in solution by vacuum ultraviolet circular dichroism. J. Mol. Biol. 138, 149178.
  • Brandl, C.J., deLeon, S., Martin, D.R., & MacLennan, D.H. (1987). Adult forms of the Ca2+ ATPase of sarcoplasmic reticlum. J. Biol. Chem. 262, 37683774.
  • Brandl, C.J., Green, N.M., Korczak, B., & MacLennan, D.H. (1986). Two Ca2+ ATPase genes: Homologies and mechanistic implications of deduced amino acid sequences. Cell 44, 597607.
  • Brith-Lindner, M. & Rosenheck, K. (1977). The circular dichroism of bacteriorhodopsin: Asymmetry and light scattering distortions. FEBS Lett. 76, 4144.
  • Brunden, K.R., Uratani, Y., & Cramer, W.A. (1984). Dependence of the conformation of a colicin El channel-forming peptide on acidic pH and solvent polarity. J. Biol. Chem. 259, 76827687.
  • Capaldi, R.A. (1990). Structure and function of cytochrome C oxidase. Annu. Rev. Biochem. 59, 569596.
  • Casey, J.R., Lieberman, D.M., & Reithmeier, R.A.F. (1989). Purification and characterization of Band 3 protein. Methods Enzymol. 173, 494512.
  • Casey, J.R. & Reithmeier, R.A.F. (1991). Analysis of the oligomeric state of Band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography. J. Biol. Chem. 266, 1572615737.
  • Chang, C.-H., Tiede, D., Tang, J., Smith, U., Norris, J., & Schiffer, M. (1986). Structure of Rhodopseudomonas sphaeroides R-26 reaction center. FEBS Lett. 205, 8286.
  • Chang, C.T., Wu, C.-S.C., & Yang, J.T. (1978). Circular dichroism analysis of protein conformation: Inclusion of the β-turns. Anal. Biochem. 91, 1331.
  • Chen, Y.-H., Yang, J.T., & Chau, K.H. (1974). Determination of the helix and β-form of proteins in aqueous solution by circular dichroism. Biochemistry 13, 33503359.
  • Chin, J.J., Jung, E.K.Y., Chen, V., & Jung, C.Y. (1987). Structural basis of human erythrocyte glucose transporter function in proteoliposome vesicles: Circular dichroism measurements. Proc. Natl. Acad. Sci. USA 84, 41134116.
  • Chou, P.Y. & Fasman, G.D. (1974). Prediction of protein conformation. Biochemistry 13, 222245.
  • Chou, P.Y. & Fasman, G.D. (1977). β-Turns in proteins. J. Mol. Biol. 115, 135175.
  • Cleveland, M.B., Slatin, S., Finkelstein, A., & Levinthal, C. (1983). Structure-function relationships for a voltage-dependent ion channel: Properties of COOH terminal fragments of colicin El. Proc. Natl. Acad. Sci. USA 80, 37063710.
  • Cogdell, R.J. & Scheer, H. (1985). Circular dichroism of light harvesting complexes from purple photosynthetic bacteria. Photochem. Photobiol. 42, 669678.
  • Cogdell, R.J., Woolley, K.J., Ferguson, L.A., & Dawkins, D.J. (1990). Crystallization of purple bacterial antenna complexes. In Crystallization of Membrane Proteins (Michel, H., Ed.), pp. 125136. CRC Press, Boca Raton, Florida.
  • Cogdell, R.J., Woolley, K., McKenzie, R.C., Lindsay, J.G., Michel, H., Dobler, J., & Zinth, W. (1985). Crystallization of the B800–850-complex from Rhodopseudomonas acidophila strain 7750. In Antennas and Reaction Centers of Photosynthetic Bacteria (Michel-Beyerle, M.E., Ed.), pp. 8587. Springer-Verlag, New York.
  • Cross, R.L. (1988). The number of functional catalytic sites on F1 ATPases and the effects of quaternary structural asymmetry on their properties. J. Bioenerg. Biomembr. 20, 395405.
  • Dankert, J.R., Uratani, Y., Grabau, C., Cramer, W.A., & Hermodson, M. (1982). On a domain structure of colicin El. J. Biol. Chem. 257, 38573863.
  • Davidson, V.L., Brunden, K.R., Cramer, W.A., & Cohen, F.S. (1984). Studies on the mechanism of action of channel-forming colicins using artificial membranes. J. Membr. Biol. 79, 105118.
  • Deisenhofer, J., Epp, O., Miki, K., Huber, R., & Michel, H. (1985). Structure of the protein subunits in the photosynthetic reaction center of Rhodopseudomonas viridis at 3 Å resolution. Nature 318, 618624.
  • Deisenhofer, J., Epp, O., Miki, K., Huber, R., & Michel, H. (1984). X-ray structure analysis of a membrane protein complex. Electron density map at 3 Å resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J. Mol. Biol. 180, 385398.
  • Deisenhofer, J. & Michel, H. (1989). The photosynthetic reaction center from the purple bacterium Rhodopseudomonas viridis. Science 245, 14631473.
  • Dencher, N.A. & Heyn, M.P. (1978). Formation and properties of bacteriorhodopsin monomers in the non-ionic detergents octyl-β-d-glucoside and Triton X-100. FEBS Lett. 96, 322326.
  • Duysens, L.N.M. (1956). The flattening of the absorption spectrum of suspensions, as compared to that of solutions. Biochim. Biophys. Acta 19, 112.
  • Falson, P., Di Pietro, A., Jault, J.-M., & Gautheron, D.C. (1986). Chemical modification of thiol group of mitochondrial F1-ATPase from the yeast Schizosaccharomyces pombe. J. Biol. Chem. 261, 71517159.
  • Falson, P., Di Pietro, A., Jault, J.-M., Gautheron, D.C., & Boutry, M. (1989). Purification from a yeast mutant of mitochondrial F1 with modified β-subunit. High affinity for nucleotides and high negative cooperativity of ATPase activity. Biochim. Biophys. Acta 975, 119126.
  • Feher, G., Allen, J.P., Okamura, M.Y., & Rees, D.C. (1989). Structure and function of bacterial photosynthetic reaction centers. Nature 339, 111116.
  • Foster, D.L. & Fillingame, R.H. (1979). Energy-transducing H+-ATPase of Escherichia coli. J. Biol. Chem. 254, 82308236.
  • Fulmer, A.W. (1979). Studies on chromatin reconstitution. Ph.D. Thesis, Brandeis University, Waltham, Massachusetts.
  • Garavito, R.M. & Rosenbusch, J.P. (1986). Isolation and crystallization of bacterial porin. Methods Enzymol. 125, 309328.
  • Glaeser, R.M. & Jap, B.K. (1985). Absorption flattening in the circular dichroism spectra of small membrane fragments. Biochemistry 24, 63986401.
  • Gordon, D.J. & Holzwarth, G. (1971). Artifacts in the measured optical activity of membrane suspensions. Arch. Biochem. Biophys. 142, 481488.
  • Greenfield, N. & Fasman, G.D. (1969). Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8, 41084116.
  • Harbison, G.S., Smith, S.O., Pardoen, J.A., Courtin, J.M.L., Lugtenburg, J., Herzfeld, J., Mathies, R.A., & Griffin, R.G. (1985). Solid-state 13C NMR detection of a perturbed 6-s-trans chromophore in bacteriorhodopsin. Biochemistry 24, 69556962.
  • Helenius, A., McCaslin, D.R., Fries, E., & Tanford, C. (1979). Properties of detergents. Methods Enzymol. 56, 734749.
  • Henderson, R., Baldwin, J.M., Ceska, T.A., Zemlin, F., Beckmann, E., & Downing, K.H. (1990). Model for the structure of bacteriorhodopsin based on high-resolution electron cryomicroscopy. J. Mol. Biol. 213, 899929.
  • Hennessey, J.P. Jr., & Johnson, W.C. Jr., (1981). Information content in the circular dichroism of proteins. Biochemistry 20, 10851094.
  • Hollósi, M., Kövér, K.E., Holly, S., & Fasman, G.D. (1987a). β-Turns in serine-containing linear and cyclic peptide models. Biopolymers 26, 15271533.
  • Hollósi, M., Kövér, K.E., Holly, S., Radics, L., & Fasman, G.D. (1987b). β-Turns in bridged proline-containing cyclic peptide models. Biopolymers 26, 15551572.
  • Holzwarth, G. & Doty, P. (1965). The ultraviolet circular dichroism of polypeptides. J. Am. Chem. Soc. 87, 218228.
  • Johnson, W.C. Jr., (1990). Protein secondary structure and circular dichroism: A practical guide. Proteins 7, 205214.
  • Kleffel, B., Garavito, R.M., Baumeister, W., & Rosenbusch, J.P. (1985). Secondary structure of a channel-forming protein: Porin from E. coli outer membranes. EMBO J. 4, 15891592.
  • Kreusch, A., Weiss, M.S., Welte, W., Weckesser, J., & Schulz, G.E. (1991). Crystals of an integral membrane protein diffracting to 1.8 Å resolution. J. Mol. Biol. 217, 910.
  • Kühlbrandt, W. (1988). Three-dimensional crystallization of membrane proteins. Q. Rev. Biophys. 21 (4), 429477.
  • Lakey, J.H., Massotte, D., Heitz, F., Dasseux, J.-L., Faucon, J.-F., Parker, M.W., & Pattus, F. (1991). Membrane insertion of the poreforming domain of colicin A: A spectroscopic study. Eur. J. Biochem. 196, 599607.
  • Lee, N., Cheng, E., & Inouye, M. (1977). Optical properties of an outer membrane lipoprotein from Escherichia coli. Biochim. Biophys. Acta 465, 650656.
  • Long, M.M., Urry, D.W., & Stoeckenius, W. (1977). Circular dichroism of biological membranes: Purple membrane of Halobacterium halobium. Biochem. Biophys. Res. Commun. 75, 725731.
  • MacLennan, D.H., Brandl, C.J., Korczak, B., & Green, N.M. (1985). Amino-acid sequence of a Ca2+–Mg2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum deduced from its complementary DNA sequence. Nature 316, 696700.
  • Madden, T.D., Chapman, D., & Quinn, P.J. (1979). Cholesterol modulates activity of calcium dependent-ATPase of the sarcoplasmic reticulum. Nature 279, 538541.
  • Manavalan, P. & Johnson, W.C. Jr., (1987). Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra. Anal. Biochem. 167, 7685.
  • Manning, M.C., Illangasekare, M., & Woody, R.W. (1988). Circular dichroism studies of distorted α-helices, twisted β-sheets, and β-turns. Biophys. Chem. 31, 7786.
  • Mao, D. & Wallace, B.A. (1984). Differential light scattering and absorption flattening optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles. Biochemistry 23, 26672673.
  • McRee, D.E., Tainer, J.A., Meyer, T.E., van Beeumen, J., Cusanovich, M., & Getzoff, E.D. (1989). Crystallographic structure of a photoreceptor protein at 2.4 Å resolution. Proc. Natl. Acad. Sci. USA 86, 65336537.
  • Mendel-Hartvig, J. & Capaldi, R.A. (1991). Catalytic site nucleotide and inorganic phosphate dependence of the conformation of the ϵ subunit in Escherichia coli adenosinetriphosphatase. Biochemistry 30, 12781284.
  • Mollevanger, L.C.P.J., Kentgens, A.P.M., Pardoen, J.A., Courtin, J.M.L., Veeman, W.S., Lugtenburg, J., & de Grip, W.J. (1987). High-resolution solid-state 13C-NMR study of carbons C-5 and C-12 of the chromophore of bovine rhodopsin. Eur. J. Biochem. 163, 914.
  • Nabedryk, E., Berger, G., Andrianambinintsoa, S., & Breton, J. (1985). Comparison of α helix orientation in chromatophore, quantasome and reaction center of Rhodopseudomonas viridis by circular dichroism and polarized infrared spectroscopy. Biochim. Biophys. Acta 809, 271276.
  • Nabedryk, E., Tiede, D.M., Dutton, P.L., & Breton, J. (1982). Conformation and orientation of the protein in the bacterial photosynthetic reaction center. Biochim. Biophys. Acta 682, 273280.
  • Némethy, G., Philips, D.C., Leach, S.J., & Scheraga, H.A. (1967). A second right-handed helical structure with the parameters of the Pauling-Corey α helix. Nature 214, 363365.
  • Ohno-Iwashita, Y. & Imahori, K. (1982). Assignment of the functional loci in the colicin E1 molecule by characterization of its proteolytic fragments. J. Biol. Chem. 257, 64466451.
  • Oikawa, K., Lieberman, D.M., & Reithmeier, R.A.F. (1985). Conformation and stability of the anion transport protein of human erythrocyte membranes. Biochemistry 24, 28432848.
  • Pancoska, P. & Keiderling, T.A. (1991). Systematic comparison of statistical analyses of electronic and vibrational circular dichroism for secondary structure prediction of selected proteins. Biochemistry 30, 68856895.
  • Papiz, M.Z., Hawthornthwaite, A.M., Cogdell, R.J., Woolley, K.J., Wightrian, P.A., Ferguson, L.A., & Lindsay, J.G. (1989). Crystallization and characterization of two crystal forms of the B800–850 light harvesting complex from Rhodopseudomonas acidophila strain 10050. J. Mol. Biol. 209, 833835.
  • Parker, M.W., Pattus, F., Tucker, A.D., & Tsernoglou, D. (1989). Structure of the membrane-pore-forming fragment of colicin A. Nature 337, 9396.
  • Pattus, F., Heitz, F., Martinez, C., Provencher, S.W., & Lazdunski, C. (1985). Secondary structure of the pore-forming colicin A and its C-terminal fragment. Experimental fact and structure prediction. Eur. J. Biochem. 152, 681689.
  • Paul, C. & Rosenbusch, J.P. (1985). Folding patterns of porin and bacteriorhodopsin. EMBO J. 4, 15931597.
  • Penin, F., Codinot, C., & Gautheron, D.C. (1979). Optimization of the purification of mitochondrial F1 adenosine triphosphatase. Biochim. Biophys. Acta 548, 6371.
  • Perczel, A. & Fasman, G.D. (1992). Quantitative analysis of cyclic β-turn models. The effect of ring stress on β-turn geometries. Protein Sci. 1, 378395.
  • Perczel, A., Hollósi, M., Foxman, B.M., & Fasman, G.D. (1991a). Conformational analysis of pseudo cyclic hexapeptides based on quantitative circular dichroism (CD), NOE, and X-ray data. J. Am. Chem. Soc. 113, 97729784.
  • Perczel, A., Hollósi, M., Sandor, P., & Fasman, G.D. (1992a). Mixtures of type I and type II β-turn conformers showing helix-like (class C) circular dichroism spectra. Int. J. Peptide Protein Res. (in press).
  • Perczel, A., Hollósi, M., Tusnady, G., & Fasman, G.D. (1991b). Convex constraint analysis: A natural deconvolution of circular dichroism curves of proteins. Protein Eng. 4, 669679.
  • Perczel, A., Hollósi, M., Tusnady, G., & Fasman, G.D. (1989). Convex constraint decomposition of circular dichroism curves of proteins. Croatica Chim. Acta 62, 189200.
  • Perczel, A., Park, K., & Fasman, G.D. (1992b). Deconvolution of the circular dichroism spectra of proteins: The circular dichroism spectra of the antiparallel β-sheet in proteins. Proteins Struct. Funct. Genet. 13, 5769.
  • Perczel, A., Park, K., & Fasman, G.D. (1992c). Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: A practical guide. Anal. Biochem. 203, 8393.
  • Pimplikar, S.W. & Reithmeier, R.A.F. (1986). Affinity chromatography of Band 3, the anion transport protein of erythrocyte membranes. J. Biol. Chem. 261, 97709778.
  • Provencher, S.W. & Glöckner, J. (1981). Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20, 3337.
  • Rafferty, C.N., Cassim, J.Y., & McConnell, D.G. (1977). Circular dichroism, optical rotatory dispersion, and absorption studies on the conformation of bovine rhodopsin in situ and solubilized with detergents. Biophys. Struct. Mechanism 2, 277320.
  • Rath, P., Bousché, O., Merrill, A R., Cramer, W.A., & Rothchild, K.J. (1991). Fourier transform infrared evidence for a predominantly alpha-helical structure of the membrane bound channel forming COOH terminal peptide of colicin El. Biophys. J. 59, 516522.
  • Reynolds, J.A. & Stoeckenius, W. (1977). Molecular weight of bacteriorhodopsin solubilized in Triton X-100. Proc. Natl. Acad. Sci. USA 74, 28032804.
  • Sarkar, P.K. & Doty, P. (1966). The optical rotatory properties of the β configuration in polypeptides and proteins. Proc. Natl. Acad. Sci. USA 55, 981989.
  • Saxena, V.P. & Wetlaufer, D.B. (1971). A new basis for interpreting the circular dichroic spectra of proteins. Proc. Natl. Acad. Sci. USA 68, 969972.
  • Schneider, A.S. & Rosenheck, K. (1982). Circular dichroism of membrane proteins. In Techniques in Lipid and Membrane Biochemistry, Part II, B424, pp. 126. Elsevier Science Publishers Ireland Ltd.
  • Senior, A.E. (1988). ATP synthesis by oxidative phosphorylation. Physiol. Rev. 68, 177231.
  • Smith, S.O., Courtin, J., van den Berg, E., Winkel, C., Lugtenburg, J., Herzfeld, J., & Griffin, R.G. (1989) Solid-state 13C NMR of the retinal chromophore in photointermediates of bacteriorhodopsin: Characterization of two forms of M. Biochemistry 28, 237243.
  • Smith, S.O. & Griffin, R.G. (1988). High-resolution solid-state NMR of proteins. Annu. Rev. Phys. Chem. 39, 511535.
  • Smith, S.O., Palings, I., Copie, V., Raleigh, D.P., Courtin, J., Pardoen, J.A., Lugtenburg, J., Mathies, R.A., & Griffin, R.G. (1987). Low-temperature solid-state 13C NMR studies of the retinal chromophore in rhodopsin Biochemistry 26, 16061611.
  • Tinoco, I. Jr., Woody, R.W., & Bradley, D.F. (1963). Absorption and rotation of light by helical polymers: The effect of chain lengths. J. Chem. Phys. 38, 13171325.
  • Urry, D.W. & Long, M.M. (1980). Ultraviolet absorption, circular dichroism, and optical rotatory dispersion in biomembrane studies. In Membrane Physiology (Andreoli, T.E., Hoffman, J.F., & Fanestil, D.D., Eds.), pp. 107124. Plenum Medical Book Co., New York.
  • Vogel, H. & Jähnig, F. (1986). Models for the structure of outer membrane proteins of Escherichia coli derived from Raman spectroscopy and prediction methods. J. Mol. Biol. 190, 191199.
  • Weiss, M.S., Kreusch, A., Schiltz, E., Nestel, U., Welter, W., Weckesser, J., & Schulz, G.E. (1991). The structure of porin from Rhodobacter capsulatus at 1.8 Å resolution. FEBS Lett. 280, 379382.
  • Witt, H.T., Rögner, M., Mühlenhoff, U., Witt, I., Hinrichs, W., Saenger, W., Betzel, C., Dauter, Z., & Boekema, E.J. (1990). On isolated complexes of reaction center I and X-ray characterization of single crystals. In Current Research in Photosynthesis, Vol. II (Baltscheffsky, W., Ed.), pp. 547554. Kluwer, Dordrecht.
  • Woody, R. (1974). Studies of theoretical circular dichroism of polypeptides: Contributions of β turns. In Peptides, Polypeptides and Proteins (Blout, E.R., Bovey, F.A., Goodman, M., & Lotan, N., Eds.), pp. 338350. Wiley, New York.
  • Woody, R.W. & Tinoco, I. Jr., (1967). Optical rotation of oriented helices. III. Calculation of rotatory dispersion and circular dichroism of the alpha and 310 helix. J. Chem. Phys. 46, 49274945.
  • Yamada, M., Ebina, Y., Miyata, T., Nakazawa, T., & Nakazawa, A. (1982). Nucleotide sequence of the structural gene for colicin El and predicted structure of the protein. Proc. Natl. Acad. Sci. USA 79, 28272831.
  • Yang, J.T., Wu, C.-S.C., & Martinez, H.M. (1986). Calculation of protein conformation from circular dichroism. Methods Enzymol. 130, 208269.
  • Yoshikawa, S., Choc, M.G., O'Toole, M.C., & Caughey, W.S. (1977). An infrared study of CO binding to heart cytochrome C oxidase and hemoglobin A. J. Biol. Chem. 252, 54985508.
  • Zhang, Y.-Z., Ewart, G., & Capaldi, R.A. (1991). Topology of subunits of the mammalian cytochrome C-oxidase: Relationship to the assembly of the enzyme complex. Biochemistry 30, 36743681.