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17 results on '"Jacob Schäfer"'

1. Rcf1 Modulates Cytochrome c Oxidase Activity Especially Under Energy-Demanding Conditions

Author

Hannah Dawitz, Jacob Schäfer, Judith M. Schaart, Wout Magits, Peter Brzezinski, and Martin Ott

Subjects
Rcf1, Rcf2, respiratory supercomplex, cytochrome c oxidase, bc1 complex, interaction partners, Physiology, QP1-981
Abstract

The mitochondrial respiratory chain is assembled into supercomplexes. Previously, two respiratory supercomplex-associated proteins, Rcf1 and Rcf2, were identified in Saccharomyces cerevisiae, which were initially suggested to mediate supercomplex formation. Recent evidence suggests that these factors instead are involved in cytochrome c oxidase biogenesis. We demonstrate here that Rcf1 mediates proper function of cytochrome c oxidase, while binding of Rcf2 results in a decrease of cytochrome c oxidase activity. Chemical crosslink experiments demonstrate that the conserved Hig-domain as well as the fungi specific C-terminus of Rcf1 are involved in molecular interactions with the cytochrome c oxidase subunit Cox3. We propose that Rcf1 modulates cytochrome c oxidase activity by direct binding to the oxidase to trigger changes in subunit Cox1, which harbors the catalytic site. Additionally, Rcf1 interaction with cytochrome c oxidase in the supercomplexes increases under respiratory conditions. These observations indicate that Rcf1 could enable the tuning of the respiratory chain depending on metabolic needs or repair damages at the catalytic site.

Published
2020
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2. Kinetic advantage of forming respiratory supercomplexes

Author

Alexei A. Stuchebrukhov, Jacob Schäfer, Johan Berg, and Peter Brzezinski

Subjects
0303 health sciences, Chemistry, Aerobic bacteria, 030302 biochemistry & molecular biology, Biophysics, Cell Biology, Biochemistry, Models, Biological, Mitochondria, Electron Transport, 03 medical and health sciences, Kinetics, Electron Transport Chain Complex Proteins, Functional significance, Respiratory Chains, Respiratory system, Biological sciences, 030304 developmental biology
Abstract

Components of respiratory chains in mitochondria and some aerobic bacteria assemble into larger, multiprotein membrane-bound supercomplexes. Here, we address the functional significance of supercomplexes composed of respiratory-chain complexes III and IV. Complex III catalyzes oxidation of quinol and reduction of water-soluble cytochrome c (cyt c), while complex IV catalyzes oxidation of the reduced cyt c and reduction of dioxygen to water. We focus on two questions: (i) under which conditions does diffusion of cyt c become rate limiting for electron transfer between these two complexes? (ii) is there a kinetic advantage of forming a supercomplex composed of complexes III and IV? To answer these questions, we use a theoretical approach and assume that cyt c diffuses in the water phase while complexes III and IV either diffuse independently in the two dimensions of the membrane or form supercomplexes. The analysis shows that the electron flux between complexes III and IV is determined by the equilibration time of cyt c within the volume of the intermembrane space, rather than the cyt c diffusion time constant. Assuming realistic relative concentrations of membrane-bound components and cyt c and that all components diffuse independently, the data indicate that electron transfer between complexes III and IV can become rate limiting. Hence, there is a kinetic advantage of bringing complexes III and IV together in the membrane to form supercomplexes.

Published
2020

3. Structure of a functional obligate complex III2IV2 respiratory supercomplex from Mycobacterium smegmatis

Author

Martin Högbom, Peter Brzezinski, Samir Benlekbir, Jacob Schäfer, Pia Ädelroth, Hui Guo, Olga Fedotovskaya, John L. Rubinstein, Dan Sjöstrand, Benjamin Wiseman, Ram Gopal Nitharwal, and Qie Kuang

Subjects
0301 basic medicine, chemistry.chemical_classification, biology, Cytochrome, Stereochemistry, Cytochrome c, Mycobacterium smegmatis, 030106 microbiology, biology.organism_classification, Electron transport chain, 03 medical and health sciences, 030104 developmental biology, Cytochrome C1, chemistry, Structural Biology, Oxidoreductase, Coenzyme Q – cytochrome c reductase, biology.protein, Electrochemical gradient, Molecular Biology
Abstract

In the mycobacterial electron-transport chain, respiratory complex III passes electrons from menaquinol to complex IV, which in turn reduces oxygen, the terminal acceptor. Electron transfer is coupled to transmembrane proton translocation, thus establishing the electrochemical proton gradient that drives ATP synthesis. We isolated, biochemically characterized, and determined the structure of the obligate III2IV2 supercomplex from Mycobacterium smegmatis, a model for Mycobacterium tuberculosis. The supercomplex has quinol:O2 oxidoreductase activity without exogenous cytochrome c and includes a superoxide dismutase subunit that may detoxify reactive oxygen species produced during respiration. We found menaquinone bound in both the Qo and Qi sites of complex III. The complex III-intrinsic diheme cytochrome cc subunit, which functionally replaces both cytochrome c1 and soluble cytochrome c in canonical electron-transport chains, displays two conformations: one in which it provides a direct electronic link to complex IV and another in which it serves as an electrical switch interrupting the connection.

Published
2018
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4. Structural and functional heterogeneity of cytochrome c oxidase in S. cerevisiae

Author

Martin Ott, Pia Ädelroth, Peter Brzezinski, Jacob Schäfer, and Hannah Dawitz

Subjects
0301 basic medicine, Saccharomyces cerevisiae Proteins, Protein Conformation, Protein subunit, Kinetics, Saccharomyces cerevisiae, Biophysics, Respiratory chain, Biochemistry, Electron Transport Complex IV, Structure-Activity Relationship, 03 medical and health sciences, Electron transfer, Catalytic Domain, Cytochrome c oxidase, 030102 biochemistry & molecular biology, biology, Chemistry, Cell Biology, Ligand (biochemistry), biology.organism_classification, Oxygen, 030104 developmental biology, Membrane protein, Mitochondrial Membranes, Mutation, biology.protein
Abstract

Respiration in Saccharomyces cerevisiae is regulated by small proteins such as the respiratory supercomplex factors (Rcf). One of these factors (Rcf1) has been shown to interact with complexes III (cyt. bc1) and IV (cytochrome c oxidase, CytcO) of the respiratory chain and to modulate the activity of the latter. Here, we investigated the effect of deleting Rcf1 on the functionality of CytcO, purified using a protein C-tag on core subunit 1 (Cox1). Specifically, we measured the kinetics of ligand binding to the CytcO catalytic site, the O2-reduction activity and changes in light absorption spectra. We found that upon removal of Rcf1 a fraction of the CytcO is incorrectly assembled with structural changes at the catalytic site. The data indicate that Rcf1 modulates the assembly and activity of CytcO by shifting the equilibrium of structural sub-states toward the fully active, intact form.

Published
2018
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5. Pioneers of Magnetic Resonance

Author

E. Thomas Strom, Vera V. Mainz, Carmen J. Giunta, H. N. Cheng, Gregory S. Girolami, Pierre Laszlo, Jacob Schaefer, David E. Lewis, James R. Norris, Jack H. Freed, Lawrence J. Berliner, Alex I. Smirnov, Sandra S. Eaton, Gareth R. Eaton, E. Thomas Strom, Vera V. Mainz, Carmen J. Giunta, H. N. Cheng, Gregory S. Girolami, Pierre Laszlo, Jacob Schaefer, David E. Lewis, James R. Norris, Jack H. Freed, Lawrence J. Berliner, Alex I. Smirnov, Sandra S. Eaton, and Gareth R. Eaton

Subjects
Nuclear magnetic resonance--History--Congresses, Magnetic resonance--History--Congresses
Abstract

'This book is about Pioneers of Magnetic Resonance'--

Published
2020

6. Structure of a functional obligate complex III

Author

Benjamin, Wiseman, Ram Gopal, Nitharwal, Olga, Fedotovskaya, Jacob, Schäfer, Hui, Guo, Qie, Kuang, Samir, Benlekbir, Dan, Sjöstrand, Pia, Ädelroth, John L, Rubinstein, Peter, Brzezinski, and Martin, Högbom

Subjects
Electron Transport, Models, Molecular, Oxygen, Electron Transport Complex III, Electron Transport Chain Complex Proteins, Cell Respiration, Cryoelectron Microscopy, Mycobacterium smegmatis, Oxidation-Reduction, Protein Structure, Tertiary
Abstract

In the mycobacterial electron-transport chain, respiratory complex III passes electrons from menaquinol to complex IV, which in turn reduces oxygen, the terminal acceptor. Electron transfer is coupled to transmembrane proton translocation, thus establishing the electrochemical proton gradient that drives ATP synthesis. We isolated, biochemically characterized, and determined the structure of the obligate III

Published
2018

7. Regulation of cytochrome c oxidase activity by modulation of the catalytic site

Author

Jacob Schäfer, Hannah Dawitz, Martin Ott, Pia Ädelroth, and Peter Brzezinski

Subjects
lcsh:R, Imidazoles, lcsh:Medicine, Electrons, Saccharomyces cerevisiae, Ligands, Models, Biological, Article, Electron Transport Complex IV, Oxygen, Catalytic Domain, lcsh:Q, lcsh:Science, Oxidation-Reduction
Abstract

The respiratory supercomplex factor 1 (Rcf 1) in Saccharomyces cerevisiae binds to intact cytochrome c oxidase (CytcO) and has also been suggested to be an assembly factor of the enzyme. Here, we isolated CytcO from rcf1Δ mitochondria using affinity chromatography and investigated reduction, inter-heme electron transfer and ligand binding to heme a 3. The data show that removal of Rcf1 yields two CytcO sub-populations. One of these sub-populations exhibits the same functional behavior as CytcO isolated from the wild-type strain, which indicates that intact CytcO is assembled also without Rcf1. In the other sub-population, which was shown previously to display decreased activity and accelerated ligand-binding kinetics, the midpoint potential of the catalytic site was lowered. The lower midpoint potential allowed us to selectively reduce one of the two sub-populations of the rcf1Δ CytcO, which made it possible to investigate the functional behavior of the two CytcO forms separately. We speculate that these functional alterations reflect a mechanism that regulates O2 binding and trapping in CytcO, thereby altering energy conservation by the enzyme.

Published
2018

9. Isolation of yeast complex IV in native lipid nanodiscs

Author

Irina A. Smirnova, Martin Högbom, Henrik Östbye, Jacob Schäfer, Peter Brzezinski, Christoph von Ballmoos, Fei Li, Gabriel C. Lander, Pia Ädelroth, Markus L. Björck, and Dan Sjöstrand

Subjects
0301 basic medicine, Biophysics, 02 engineering and technology, Saccharomyces cerevisiae, Mitochondrion, Biology, Biochemistry, Article, Electron Transport Complex IV, 03 medical and health sciences, Affinity chromatography, Catalytic Domain, Amphiphile, 540 Chemistry, Cytochrome c oxidase, Inner mitochondrial membrane, Cytochrome bc1, Maleates, Cell Biology, 021001 nanoscience & nanotechnology, Lipids, 030104 developmental biology, Membrane, Membrane protein, biology.protein, Nanoparticles, Polystyrenes, 570 Life sciences, biology, 0210 nano-technology
Abstract

We used the amphipathic styrene maleic acid (SMA) co-polymer to extract cytochrome c oxidase (CytcO) in its native lipid environment from S. cerevisiae mitochondria. Native nanodiscs containing one CytcO per disc were purified using affinity chromatography. The longest cross-sections of the native nanodiscs were 11 nm × 14 nm. Based on this size we estimated that each CytcO was surrounded by ~100 phospholipids. The native nanodiscs contained the same major phospholipids as those found in the mitochondrial inner membrane. Even though CytcO forms a supercomplex with cytochrome bc(1) in the mitochondrial membrane, cyt. bc(1) was not found in the native nanodiscs. Yet, the loosely-bound Respiratory SuperComplex factors were found to associate with the isolated CytcO. The native nanodiscs displayed an O(2)-reduction activity of ~130 electrons CytcO(−1) s(−1) and the kinetics of the reaction of the fully reduced CytcO with O(2) was essentially the same as that observed with CytcO in mitochondrial membranes. The kinetics of CO-ligand binding to the CytcO catalytic site was similar in the native nanodiscs and the mitochondrial membranes. We also found that excess SMA reversibly inhibited the catalytic activity of the mitochondrial CytcO, presumably by interfering with cyt. c binding. These data point to the importance of removing excess SMA after extraction of the membrane protein. Taken together, our data shows the high potential of using SMA-extracted CytcO for functional and structural studies.

Published
2016
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10. Cysteine scanning reveals minor local rearrangements of the horizontal helix of respiratory complex I

Author

Stefan Steimle, Jacob Schäfer, Bartlomiej Matlosz, Udo Glessner, Katharina Maurer, Thorsten Friedrich, Sofia Brander, Christian Schnick, Hannah Dawitz, Franziska Nuber, Eva-Maria Burger, and Dorothée Krämer

Subjects
Models, Molecular, Ubiquinone, Biology, Microbiology, Redox, Spin probe, Electron Transport, Electron transfer, Oxidoreductase, Escherichia coli, Cysteine, Molecular Biology, chemistry.chemical_classification, Electron Transport Complex I, Escherichia coli Proteins, Electron Spin Resonance Spectroscopy, NADH Dehydrogenase, NAD, Fluorescence, Membrane, chemistry, Biochemistry, Helix, Mutation, Biophysics, Protons, Oxidation-Reduction
Abstract

Summary The NADH:ubiquinone oxidoreductase, respiratory complex I, couples electron transfer from NADH to ubiquinone with the translocation of protons across the membrane. The complex consists of a peripheral arm catalyzing the redox reaction and a membrane arm catalyzing proton translocation. The membrane arm is almost completely aligned by a 110 A unique horizontal helix that is discussed to transmit conformational changes induced by the redox reaction in a piston-like movement to the membrane arm driving proton translocation. Here, we analyzed such a proposed movement by cysteine-scanning of the helix of the Escherichia coli complex I. The accessibility of engineered cysteine residues and the flexibility of individual positions were determined by labeling the preparations with a fluorescent marker and a spin-probe, respectively, in the oxidized and reduced states. The differences in fluorescence labeling and the rotational flexibility of the spin probe between both redox states indicate only slight conformational changes at distinct positions of the helix but not a large movement.

Published
2015

11. Molecular Sieves—II

Author

JAMES R. KATZER, M. M. DUBININ, G. V. GIBBS, E. P. MEAGHER, J. V. SMITH, J. J. PLUTH, JOHN D. SHERMAN, W. H. FLANK, H. LECHERT, H. W. HENNEKE, R. L. PATTON, E. M. FLANIGEN, L. G. DOWELL, D. E. PASSOJA, J-FR. TEMPERE, D. DELAFOSSE, J. P. CONTOUR, C. DEFOSSE, B. DELMON, P. CANESSON, G. H. KÜHL, KAMIL KLIER, PAUL J. HUTTA, RICHARD KELLERMAN, WILLY DE WILDE, ROBERT A. SCHOONHEYDT, JAN B. UYTTERHOEVEN, P. GALLEZOT, G. COUDURIER, M. PRIMET, B. IMELIK, CLAUDE NACCACHE, YOUNÈS BEN TAARIT, MICHEL BOUDART, LOVAT V. C. REES, PAUL A. NEWELL, ADRIEN CREMERS, C. L. ANGELL, ANIL K. PATEL, L. B. SAND, DAVID T. HAYHURST, HARRY E. ROBSON, KENNETH L. RILEY, DALE D. MANESS, HARTMUT KACIREK, HANS LECHERT, R. M. BARRER, R. G. JENKINS, G. PEETERS, D. W. BRECK, G. W. SKEELS, EDOUARD GARBOWSKI, MICHEL PRIMET, MICHEL-VITAL MATHIEU, F. SCHMIDT, W. GUNSSER, J. ADOLPH, W. SCHIRMER, K. FIEDLER, H. STACH, DOUGLAS M. RUTHVEN, W. D. BASLER, M. D. SEFCIK, JACOB SCHAEFER, E. O. STEJSKAL, R. SCHÜLLNER, H.-J. HERDEN, PIERRE CARTRAUD, ANDRÉ COINTOT, BERNARD CHAUVEAU, K. A. HOLBOROW, K. F. LOU, JAMES R. KATZER, M. M. DUBININ, G. V. GIBBS, E. P. MEAGHER, J. V. SMITH, J. J. PLUTH, JOHN D. SHERMAN, W. H. FLANK, H. LECHERT, H. W. HENNEKE, R. L. PATTON, E. M. FLANIGEN, L. G. DOWELL, D. E. PASSOJA, J-FR. TEMPERE, D. DELAFOSSE, J. P. CONTOUR, C. DEFOSSE, B. DELMON, P. CANESSON, G. H. KÜHL, KAMIL KLIER, PAUL J. HUTTA, RICHARD KELLERMAN, WILLY DE WILDE, ROBERT A. SCHOONHEYDT, JAN B. UYTTERHOEVEN, P. GALLEZOT, G. COUDURIER, M. PRIMET, B. IMELIK, CLAUDE NACCACHE, YOUNÈS BEN TAARIT, MICHEL BOUDART, LOVAT V. C. REES, PAUL A. NEWELL, ADRIEN CREMERS, C. L. ANGELL, ANIL K. PATEL, L. B. SAND, DAVID T. HAYHURST, HARRY E. ROBSON, KENNETH L. RILEY, DALE D. MANESS, HARTMUT KACIREK, HANS LECHERT, R. M. BARRER, R. G. JENKINS, G. PEETERS, D. W. BRECK, G. W. SKEELS, EDOUARD GARBOWSKI, MICHEL PRIMET, MICHEL-VITAL MATHIEU, F. SCHMIDT, W. GUNSSER, J. ADOLPH, W. SCHIRMER, K. FIEDLER, H. STACH, DOUGLAS M. RUTHVEN, W. D. BASLER, M. D. SEFCIK, JACOB SCHAEFER, E. O. STEJSKAL, R. SCHÜLLNER, H.-J. HERDEN, PIERRE CARTRAUD, ANDRÉ COINTOT, BERNARD CHAUVEAU, K. A. HOLBOROW, and K. F. LOU

Subjects
Zeolites--Congresses, Molecular sieves--Congresses
Published
1977

12. NMR Spectroscopy: New Methods and Applications

Author

GEORGE C. LEVY, DAVID J. CRAIK, FELIX W. WEHRLI, A. A. BOTHNER-BY, J. DADOK, R. R. ERNST, PIERRE LASZLO, IAN C. P. SMITH, HENRY H. MANTSCH, ROBERT E. LONDON, N. A. MATWIYOFF, R. E. LONDON, J. Y. HUTSON, JACOB SCHAEFER, E. O. STEJSKAL, R. A. McKAY, JIRI JONAS, WILLIAM H. DAWSON, STEVE W. KAISER, RUTH R. INNERS, F. DAVID DOTY, PAUL D. ELLIS, L. M. GIERASCH, M. H. FREY, J. G. HEXEM, S. J. OPELLA, JACK S. COHEN, CHI-WAN CHEN, PETER R. HILLIARD, RANDOLPH L. RILL, LINDA F. LEVY, P. J. HORE, R. KAPTEIN, GARY E. MACIEL, MARK J. SULLIVAN, LYNN W. JELINSKI, JOSEPH J. DUMAIS, F. C. SCHILLING, F. A. BOVEY, GEORGE C. LEVY, DAVID J. CRAIK, FELIX W. WEHRLI, A. A. BOTHNER-BY, J. DADOK, R. R. ERNST, PIERRE LASZLO, IAN C. P. SMITH, HENRY H. MANTSCH, ROBERT E. LONDON, N. A. MATWIYOFF, R. E. LONDON, J. Y. HUTSON, JACOB SCHAEFER, E. O. STEJSKAL, R. A. McKAY, JIRI JONAS, WILLIAM H. DAWSON, STEVE W. KAISER, RUTH R. INNERS, F. DAVID DOTY, PAUL D. ELLIS, L. M. GIERASCH, M. H. FREY, J. G. HEXEM, S. J. OPELLA, JACK S. COHEN, CHI-WAN CHEN, PETER R. HILLIARD, RANDOLPH L. RILL, LINDA F. LEVY, P. J. HORE, R. KAPTEIN, GARY E. MACIEL, MARK J. SULLIVAN, LYNN W. JELINSKI, JOSEPH J. DUMAIS, F. C. SCHILLING, and F. A. BOVEY

Subjects
Nuclear magnetic resonance spectroscopy--Congres
Published
1982

13. Nitrogen-Containing Macromolecules in the Bio- and Geosphere

Author

B. ARTUR STANKIEWICZ, PIM F. VAN BERGEN, Karl J. Kramer, Theodore L. Hopkins, Jacob Schaefer, G. Gleixner, H.-L. Schmidt, James B. Reeves, Barry A. Francis, Jeffrey L. Bada, M. J. Collins, D. Walton, A. King, Reno T. Nguyen, H. Rodger Harvey, Helen A. Bland, James F. Carter, Richard P. Evershed, Hendrik N. Poinar, Riccardo A. A. Muzzarelli, Corrado Muzzarelli, Mathieu Poulicek, François Gaill, Gerhard Goffinet, Derek E. G. Briggs, Randall F. Miller, Anja Bierstedt, A. Schimmelmann, R. P. Wintsch, M. D. Lewan, M. J. DeNiro, S. Derenne, H. Knicker, C. Largeau, P. Hatcher, B. M. Krooss, B. Müller, P. Gerling, R. Littke, Richard A. Kohn, Stefanie Siebert, Heike Knicker, Mark A. Hatcher, Jens Leifield, Ingrid Kögel-Knabner, R. Bol, J. M. Wilson, R. S. Shiel, K. J. Petzke, A. Watson, J. Cockburn, Matthew B. Flannery, Paul R. Poulton, B. ARTUR STANKIEWICZ, PIM F. VAN BERGEN, Karl J. Kramer, Theodore L. Hopkins, Jacob Schaefer, G. Gleixner, H.-L. Schmidt, James B. Reeves, Barry A. Francis, Jeffrey L. Bada, M. J. Collins, D. Walton, A. King, Reno T. Nguyen, H. Rodger Harvey, Helen A. Bland, James F. Carter, Richard P. Evershed, Hendrik N. Poinar, Riccardo A. A. Muzzarelli, Corrado Muzzarelli, Mathieu Poulicek, François Gaill, Gerhard Goffinet, Derek E. G. Briggs, Randall F. Miller, Anja Bierstedt, A. Schimmelmann, R. P. Wintsch, M. D. Lewan, M. J. DeNiro, S. Derenne, H. Knicker, C. Largeau, P. Hatcher, B. M. Krooss, B. Müller, P. Gerling, R. Littke, Richard A. Kohn, Stefanie Siebert, Heike Knicker, Mark A. Hatcher, Jens Leifield, Ingrid Kögel-Knabner, R. Bol, J. M. Wilson, R. S. Shiel, K. J. Petzke, A. Watson, J. Cockburn, Matthew B. Flannery, and Paul R. Poulton

Published
1998

14. Biotechnology for Crop Protection

Author

PAUL A. HEDIN, JULIUS J. MENN, ROBERT M. HOLLINGWORTH, J. Gressel, Y. Shaaltiel, Julie K. Smith, C. Jeffry Mauvais, Susan Knowlton, Barbara J. Mazur, G. Kishore, D. Shah, S. Padgette, G. della-Cioppa, C. Gasser, D. Re, C. Hironaka, M. Taylor, J. Wibbenmeyer, D. Eichholtz, M. Hayford, N. Hoffmann, X. Delannay, R. Horsch, H. Klee, S. Rogers, D. Rochester, L. Brundage, P. Sanders, R. T. Fraley, Horace G. Cutler, R. J. Cole, J. W. Dorner, P. D. Blankenship, T. H. Sanders, Richard C. Staples, Harvey C. Hoch, Albert Stoessl, Z. Abramowski, H. H. Lester, G. L. Rock, J. B. Stothers, G. H. N. Towers, R. C. Zimmer, George M. Strunz, Douglas B. Strongman, J. David Miller, Roy Greenhalgh, Paul D. Shirk, David A. O'Brochta, P. Elaine Roberts, Alfred M. Handler, Larry L. Keeley, Karl J. Kramer, Theodore L. Hopkins, Jacob Schaefer, John H. Postlethwait, Stephen Saul, Mark Robertson, Dale Grace, Kristie Abrams, Ellie Brandenburg, Douglas C. Knipple, Jeffrey R. Bloomquist, David M. Soderlund, András Székács, Bruce D. Hammock, Yehia A. I. Abdel-Aal, Matthew Philpott, Gy, PAUL A. HEDIN, JULIUS J. MENN, ROBERT M. HOLLINGWORTH, J. Gressel, Y. Shaaltiel, Julie K. Smith, C. Jeffry Mauvais, Susan Knowlton, Barbara J. Mazur, G. Kishore, D. Shah, S. Padgette, G. della-Cioppa, C. Gasser, D. Re, C. Hironaka, M. Taylor, J. Wibbenmeyer, D. Eichholtz, M. Hayford, N. Hoffmann, X. Delannay, R. Horsch, H. Klee, S. Rogers, D. Rochester, L. Brundage, P. Sanders, R. T. Fraley, Horace G. Cutler, R. J. Cole, J. W. Dorner, P. D. Blankenship, T. H. Sanders, Richard C. Staples, Harvey C. Hoch, Albert Stoessl, Z. Abramowski, H. H. Lester, G. L. Rock, J. B. Stothers, G. H. N. Towers, R. C. Zimmer, George M. Strunz, Douglas B. Strongman, J. David Miller, Roy Greenhalgh, Paul D. Shirk, David A. O'Brochta, P. Elaine Roberts, Alfred M. Handler, Larry L. Keeley, Karl J. Kramer, Theodore L. Hopkins, Jacob Schaefer, John H. Postlethwait, Stephen Saul, Mark Robertson, Dale Grace, Kristie Abrams, Ellie Brandenburg, Douglas C. Knipple, Jeffrey R. Bloomquist, David M. Soderlund, András Székács, Bruce D. Hammock, Yehia A. I. Abdel-Aal, Matthew Philpott, and Gy

Subjects
Plants, Protection of--Congresses, Plant biotechnology--Congresses
Published
1988

15. NMR and Macromolecules

Author

JAMES C. RANDALL, F. A. BOVEY, DANIEL J. O'DONNELL, JACOB SCHAEFER, M. D. SEFCIK, E. O. STEJSKAL, R. A. MCKAY, W. T. DIXON, R. E. CAIS, L. W. JELINSKI, J. J. DUMAIS, A. K. ENGEL, M. F. TARPEY, Y.-Y. LIN, ALAN ANTHONY JONES, P. T. INGLEFIELD, W. W. FLEMING, J. R. LYERLA, C. S. YANNONI, GEORGE A. GRAY, KUNIO HIKICHI, TOSHIFUMI HIRAOKI, SHINJI TAKEMURA, MUNEKI OHUCHI, ATSUO NISHIOKA, J. C. RANDALL, E. T. HSIEH, RUDOLF E. CAIS, JANET M. KOMETANI, CHARLES J. CARMAN, RICHARD A. KOMOROSKI, SAMUEL E. HORNE, HISAYA SATO, YASUYUKI TANAKA, H. JAMES HARWOOD, TENG-KO CHEN, FU-TYAN LIN, A. ZAMBELLI, P. AMMENDOLA, M. C. SACCHI, P. LOCATELLI, F. J. ZOEPFL, JOSEPH SILVERMAN, JAMES C. RANDALL, F. A. BOVEY, DANIEL J. O'DONNELL, JACOB SCHAEFER, M. D. SEFCIK, E. O. STEJSKAL, R. A. MCKAY, W. T. DIXON, R. E. CAIS, L. W. JELINSKI, J. J. DUMAIS, A. K. ENGEL, M. F. TARPEY, Y.-Y. LIN, ALAN ANTHONY JONES, P. T. INGLEFIELD, W. W. FLEMING, J. R. LYERLA, C. S. YANNONI, GEORGE A. GRAY, KUNIO HIKICHI, TOSHIFUMI HIRAOKI, SHINJI TAKEMURA, MUNEKI OHUCHI, ATSUO NISHIOKA, J. C. RANDALL, E. T. HSIEH, RUDOLF E. CAIS, JANET M. KOMETANI, CHARLES J. CARMAN, RICHARD A. KOMOROSKI, SAMUEL E. HORNE, HISAYA SATO, YASUYUKI TANAKA, H. JAMES HARWOOD, TENG-KO CHEN, FU-TYAN LIN, A. ZAMBELLI, P. AMMENDOLA, M. C. SACCHI, P. LOCATELLI, F. J. ZOEPFL, and JOSEPH SILVERMAN

Subjects
Macromolecules--Analysis--Congresses, Nuclear magnetic resonance spectroscopy--Congres
Published
1984

16. Naturally Occurring Pest Bioregulators

Author

PAUL A. HEDIN, Murray S. Blum, Daniel M. Everett, Tappey H. Jones, Henry M. Fales, Robert J. Bartelt, Patrick F. Dowd, Ronald D. Plattner, Thomas A. Coudron, Peter E. A. Teal, James H. Tumlinson, T. G. Bird, A. K. Raina, D. K. Hayes, K. J. Kramer, T. D. Morgan, T. L. Hopkins, Allyson Christensen, Jacob Schaefer, Leslie M. McDonough, Ward M. Tingey, John C. Steffens, Donald S. Walters, George G. Kennedy, Robert R. Farrar, R. K. Kashyap, Sean S. Duffey, Gary W. Felton, Jack D. Paxton, Carl A. Elliger, Anthony C. Waiss, D. Hesk, L. Collins, R. Craig, R. O. Mumma, R. C. Gueldner, Maurice E. Snook, B. R. Wiseman, N. W. Widstrom, D. S. Himmelsbach, C. E. Costello, R. F. Severson, D. M. Jackson, A. W. Johnson, V. A. Sisson, M. G. Stephenson, Christopher A. Mullin, Ali A. Alfatafta, Jody L. Harman, Anthony A. Serino, Susan L. Everett, S. Mark Lee, James A. Klocke, Mark A. Barnby, R. Bryan Yamasaki, Manuel F. Balandrin, Joel R. Coats, Laura L. Karr, Charles D. Drewes, D. Howard Miles, Vallapa Chittawong, Armando A. de la Cruz, Allen Matthew Payne, Edgardo, PAUL A. HEDIN, Murray S. Blum, Daniel M. Everett, Tappey H. Jones, Henry M. Fales, Robert J. Bartelt, Patrick F. Dowd, Ronald D. Plattner, Thomas A. Coudron, Peter E. A. Teal, James H. Tumlinson, T. G. Bird, A. K. Raina, D. K. Hayes, K. J. Kramer, T. D. Morgan, T. L. Hopkins, Allyson Christensen, Jacob Schaefer, Leslie M. McDonough, Ward M. Tingey, John C. Steffens, Donald S. Walters, George G. Kennedy, Robert R. Farrar, R. K. Kashyap, Sean S. Duffey, Gary W. Felton, Jack D. Paxton, Carl A. Elliger, Anthony C. Waiss, D. Hesk, L. Collins, R. Craig, R. O. Mumma, R. C. Gueldner, Maurice E. Snook, B. R. Wiseman, N. W. Widstrom, D. S. Himmelsbach, C. E. Costello, R. F. Severson, D. M. Jackson, A. W. Johnson, V. A. Sisson, M. G. Stephenson, Christopher A. Mullin, Ali A. Alfatafta, Jody L. Harman, Anthony A. Serino, Susan L. Everett, S. Mark Lee, James A. Klocke, Mark A. Barnby, R. Bryan Yamasaki, Manuel F. Balandrin, Joel R. Coats, Laura L. Karr, Charles D. Drewes, D. Howard Miles, Vallapa Chittawong, Armando A. de la Cruz, Allen Matthew Payne, and Edgardo

Subjects
Natural pesticides--Congresses, Bioactive compounds--Congresses
Published
1991

17. Magnetic Resonance in Colloid and Interface Science

Author

HENRY A. RESING, CHARLES G. WADE, JACK H. FREED, JOHN E. TANNER, D. G. STOUT, R. M. COTTS, H. PFEIFER, J. CHARVOLIN, B. MÉLY, L. W. REEVES, F. Y. FUJIWARA, M. SUZUKI, J. H. DAVIS, K. R. JEFFREY, M. BLOOM, M. I. VALIC, T. P. HIGGS, GORDON J. T. TIDDY, ETHNA EVERISS, J. CONARD, T. J. PINNAVAIA, M. D. SEFCIK, JACOB SCHAEFER, E. O. STEJSKAL, M. B. McBRIDE, J. SOHMA, M. SHIOTANI, D. HANEMAN, PHILIP J. CAPLAN, F. P. MIKNIS, D. A. NETZEL, B. BODDENBERG, J. A. MORENO, RAYMOND A. MACKAY, EDWARD J. POZIOMEK, RICHARD P. BARRETT, DOUGLAS F. BREWER, WALLACE S. BREY, BENJAMIN W. MARTIN, BURTON H. DAVIS, RICHARD B. GAMMAGE, V. YU. BOROVKOV, G. M. ZHIDOMIROV, V. B. KAZANSKY, J. L. BONARDET, L. C. MENORVAL, J. FRAISSARD, J. J. FRIPIAT, R. W. VAUGHAN, L. B. SCHREIBER, J. A. SCHWARZ, W. D. BASLER, LOVAT V. C. REES, EDWARD E. GENSER, H. LECHERT, H. J. HENNIG, S. ABLETT, P. J. LILLFORD, S. M. A. BAGHDADI, W. DERBYSHIRE, ROBBE C. LYON, JÜRGEN WECKESSER, JAMES A. MAGNUSON, GÖRAN LINDBLOM, HÅKAN WENNERSTRÖM,, BJÖRN LINDMAN, STANLEY J. OPELLA, DONALD J. NELSON, OLEG JARDETZKY, HENRY A. RESING, CHARLES G. WADE, JACK H. FREED, JOHN E. TANNER, D. G. STOUT, R. M. COTTS, H. PFEIFER, J. CHARVOLIN, B. MÉLY, L. W. REEVES, F. Y. FUJIWARA, M. SUZUKI, J. H. DAVIS, K. R. JEFFREY, M. BLOOM, M. I. VALIC, T. P. HIGGS, GORDON J. T. TIDDY, ETHNA EVERISS, J. CONARD, T. J. PINNAVAIA, M. D. SEFCIK, JACOB SCHAEFER, E. O. STEJSKAL, M. B. McBRIDE, J. SOHMA, M. SHIOTANI, D. HANEMAN, PHILIP J. CAPLAN, F. P. MIKNIS, D. A. NETZEL, B. BODDENBERG, J. A. MORENO, RAYMOND A. MACKAY, EDWARD J. POZIOMEK, RICHARD P. BARRETT, DOUGLAS F. BREWER, WALLACE S. BREY, BENJAMIN W. MARTIN, BURTON H. DAVIS, RICHARD B. GAMMAGE, V. YU. BOROVKOV, G. M. ZHIDOMIROV, V. B. KAZANSKY, J. L. BONARDET, L. C. MENORVAL, J. FRAISSARD, J. J. FRIPIAT, R. W. VAUGHAN, L. B. SCHREIBER, J. A. SCHWARZ, W. D. BASLER, LOVAT V. C. REES, EDWARD E. GENSER, H. LECHERT, H. J. HENNIG, S. ABLETT, P. J. LILLFORD, S. M. A. BAGHDADI, W. DERBYSHIRE, ROBBE C. LYON, JÜRGEN WECKESSER, JAMES A. MAGNUSON, GÖRAN LINDBLOM, HÅKAN WENNERSTRÖM,, BJÖRN LINDMAN, STANLEY J. OPELLA, DONALD J. NELSON, and OLEG JARDETZKY

Subjects
Colloids--Congresses, Surface chemistry--Congresses, Magnetic resonance--Congresses
Published
1976

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