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1,207 results on '"Saenger, Wolfram"'

1. Quasielastic small-angle neutron scattering from heavy water solutions of cyclodextrins

Author

Kusmin, André, Lechner, Ruep E., and Saenger, Wolfram

Subjects
Condensed Matter - Soft Condensed Matter
Abstract

We present a model for quasielastic neutron scattering (QENS) by an aqueous solution of compact and inflexible molecules. This model accounts for time-dependent spatial pair correlations between the atoms of the same as well as of distinct molecules and includes all coherent and incoherent neutron scattering contributions. The extension of the static theory of the excluded volume effect [A. K. Soper, J. Phys.:Condens. Matter 9, 2399 (1997)] to the time-dependent (dynamic) case allows us to obtain simplified model expressions for QENS spectra in the low Q region in the uniform fluid approximation. The resulting expressions describe the quasielastic small-angle neutron scattering (QESANS) spectra of D2O solutions of native and methylated cyclodextrins well, yielding in particular translational and rotational diffusion coefficients of these compounds in aqueous solution. Finally, we discuss the full potential of the QESANS analysis (that is, beyond the uniform fluid approximation), in particular, the information on solute-solvent interactions (e.g., hydration shell properties) that such an analysis can provide, in principle., Comment: accepted manuscript

Published
2017
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4. Where Water is Oxidized to Dioxygen: Structure of the Photosynthetic Mn4Ca Cluster

Author

Yano, Junko, Kern, Jan, Sauer, Kenneth, Latimer, Matthew J., Pushkar, Yulia, Biesiadka, Jacek, Loll, Bernhard, Saenger, Wolfram, Messinger, Johannes, Zouni, Athina, and Yachandra, Vittal K.

Subjects
Inorganic, organic, physical and analytical chemistry, Basic biological sciences, water-oxidation oxygen-evolution photosynthesis Mn complex
Abstract

Oxidation of water to dioxygen is catalyzed within photosystem II (PSII) by a Mn4Ca cluster, the structure of which remains elusive. Polarized extended X-ray absorption fine structure (EXAFS) measurements on PSII single crystals constrain the Mn4Ca cluster geometry to a set of three similar high-resolution structures. Combining polarized EXAFS and X-ray diffraction data, the cluster was placed within PSII taking into account the overall trend of the electron density of the metal site and the putative ligands. The structure of the cluster from the present study is unlike either the 3.0 or 3.5 Angstrom resolution X-ray structures, and other previously proposed models.

Published
2006

46. Bacterial Toxin-Antitoxin Systems as Targets for the Development of Novel Antibiotics

Author

Alonso, Juan C., primary, Balsa, Dolors, additional, Cherny, Izhack, additional, Christensen, Susanne K., additional, Espinosa, Manuel, additional, Francuski, Djordje, additional, Gazit, Ehud, additional, Gerdes, Kenn, additional, Hitchin, Ed, additional, Teresa Martín, M., additional, Nieto, Concepción, additional, Overweg, Karin, additional, Pellicer, Teresa, additional, Saenger, Wolfram, additional, Welfle, Heinz, additional, Welfle, Karin, additional, and Wells, Jerry, additional

Published
2014
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49. Regulation of synaptic inhibition by phosphodependent binding of the AP2 complex to a YECL motif in the [GABA.sub.A] receptor [gamma]2 subunit

Author

Kittler, Josef T., Chen, Guojun, Kukhtina, Viktoria, Vahedi-Faridi, Ardeschir, Gu, Zhenglin, Tretter, Verena, Smith, Katharine R., McAinsh, Kristina, Arancibia-Carcamo, I. Lorena, Saenger, Wolfram, Haucke, Volker, Yan, Zhen, and Moss, Stephen J.

Subjects
Phosphorylation -- Influence, Neural transmission -- Research, Phosphotransferases -- Properties, Endocytosis -- Influence, GABA -- Receptors, GABA -- Properties, Science and technology
Abstract

The regulation of the number of [gamma]2-subunit-containing GAB[A.sub.A] receptors (GAB[A.sub.A]RS) present at synapses is critical for correct synaptic inhibition and animal behavior. This regulation occurs, in part, by the controlled removal of receptors from the membrane in clathrin-coated vesicles, but it remains unclear how clathrin recruitment to surface [gamma]2-subunit-containing GAB[A.sub.A]RS is regulated. Here, we identify a [gamma]2-subunit-specific Yxx[phi]-type-binding motif for the clathrin adaptor protein, AP2, which is located within a site for [gamma]2-subunit tyrosine phosphorylation. Blocking GAB[A.sub.A]R-AP2 interactions via this motif increases synaptic responses within minutes. Crystallographic and biochemical studies reveal that phosphorylation of the Yxx[phi] motif inhibits AP2 binding, leading to increased surface receptor number. In addition, the crystal structure provides an explanation for the high affinity of this motif for AP2 and suggests that [gamma]2-subunit-containing heteromeric GAB[A.sub.A]RS may be internalized as dimers or multimers. These data define a mechanism for tyrosine kinase regulation of GAB[A.sub.A]R surface levels and synaptic inhibition. endocytosis | phosphorylation | structure | synaptic transmission | tyrosine kinase

Published
2008

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