Search

Your search keyword '"Hauß T"' showing total 185 results
Start Over Author "Hauß T"
185 results on '"Hauß T"'

1. Effect of alkan-1-ols on the structure of dopc model membrane

Author

Kondela T., Gallová J., Hauß T., Ivankov O., Kučerka N., and Balgavý P.

Subjects
model membrane - general anaesthetics - alkan-1-ols - small-angle neutron scattering - small-angle neutron diffraction - structure, Therapeutics. Pharmacology, RM1-950
Abstract

The effect of general anaesthetics alkan-1-ols (CnOH, where n = 10, 12, 14, 16 and 18 is the number of carbon atoms in the molecule) on the structure of dioleoylphosphatidylcholine (DOPC) model membrane was studied by small-angle neutron scattering (SANS) and small-angle neutron diffraction (SAND). Fluid bilayers were prepared at CnOH:DOPC = 0.3 molar ratio. The results of both the experiments show that bilayer thickness - a thickness parameter dg in the case of SANS and lamellar repeat distance D in the case of SAND - increases with increasing n. A coexistence of two lamellar phases with different D was detected by measuring the C18OH+DOPC oriented sample.

Published
2017
Full Text
View/download PDF

7. New sources and instrumentation for neutrons in biology

Author

Teixeira, S.C.M., Zaccai, G., Ankner, J., Bellissent-Funel, M.C., Bewley, R., Blakeley, M.P., Callow, P., Coates, L., Dahint, R., Dalgliesh, R., Dencher, N.A., Forsyth, V.T., Fragneto, G., Frick, B., Gilles, R., Gutberlet, T., Haertlein, M., Hauß, T., Häußler, W., Heller, W.T., Herwig, K., Holderer, O., Juranyi, F., Kampmann, R., Knott, R., Krueger, S., Langan, P., Lechner, R.E., Lynn, G., Majkrzak, C., May, R.P., Meilleur, F., Mo, Y., Mortensen, K., Myles, D.A.A., Natali, F., Neylon, C., Niimura, N., Ollivier, J., Ostermann, A., Peters, J., Pieper, J., Rühm, A., Schwahn, D., Shibata, K., Soper, A.K., Strässle, Th., Suzuki, J., Tanaka, I., Tehei, M., Timmins, P., Torikai, N., Unruh, T., Urban, V., Vavrin, R., and Weiss, K.

Published
2008
Full Text
View/download PDF

14. Activity and stability of a thermostable alpha-amylase compared to its mesophilic homologue: mechanisms of thermal adaptation

Author

Fitter, J., Herrmann, R., Dencher, N.A., Blume, A., and Hauss, T.

Subjects
Amylases -- Research, Enzymes -- Structure-activity relationship, Thermal analysis -- Research, Proteins -- Conformation, Biological sciences, Chemistry
Abstract

Comaparative analyses of a thermostable alpha-amylase and its mesophilic homologue show maximal catalytic activity at different temperatures with the former requiring a higher temperature. The temperatures for protein unfolding are same in both cases with the thermostable alpha-amylase exhibiting higher structural flexibility.

Published
2001

19. Interaction of Alzheimer’s disease triggering amyloid beta peptides with membranes and organelles: bioenergetical consequences

Author

Dencher, Norbert A., primary, Decker, V., additional, Dzinic, T., additional, Hauß, T., additional, Podolyak, E.Y., additional, Bogorodskiy, A., additional, Borshchevskiy, V., additional, Gordeliy, V., additional, Malyar, N.L., additional, Maslov, I., additional, Sugawa, M., additional, and Okhrimenko, I.S., additional

Published
2018
Full Text
View/download PDF

22. Structure and hydration of the m-state of the bacteriorhodopsin mutant D96N studied by neutron diffraction 1 1Edited by M. F. Moody

Author

Norbert A. Dencher, Hauss T, Giuseppe Zaccai, Martin Weik, and Dieter Oesterhelt

Subjects
Diffraction, Schiff base, biology, Hydrogen, Chemistry, Neutron diffraction, chemistry.chemical_element, Bacteriorhodopsin, chemistry.chemical_compound, Crystallography, Deprotonation, Membrane, Structural Biology, biology.protein, Molecule, Molecular Biology
Abstract

Neutron diffraction from oriented purple membrane fragments at various hydration levels, coupled with H 2 O/ 2 H 2 O exchange, was used to compare the structure and hydration of the light-adapted initial state (B-state) and the M photointermediate of bacteriorhodopsin mutant D96N. Diffraction patterns were recorded at 86%, 75% and 57% relative humidity (r.h.). Structural changes observed at 86% and 75% r.h. are absent at 57% r.h., showing that they are uncoupled from the deprotonation of the Schiff base during formation of the M-state. In a current model, the M-state consists of two substates, M 1 and M 2 . Our data suggest that the state trapped at 57% r.h. is M 1 and that M 2 is trapped at the higher r.h. values. The observed structural changes are, therefore, associated with the M 1 → M 2 transition, which can only take place at higher r.h. The difference Fourier projections of exchangeable hydrogen atoms and water molecules in the membrane plane are very similar for the B and M-states at 75% and 86% r.h. This shows that contrary to certain models, the structural changes in the M-state are not correlated with major hydration changes in the proton channel projection.

Published
1998
Full Text
View/download PDF

28. New sources and instrumentation for neutrons in biology

Author

Teixeira, S. C. M., Zaccai, G., Ankner, J., Bellissent-Funel, M. C., Bewley, R., Blakeley, M. P., Callow, P., Coates, L., Dahint, R., Dalgliesh, R., Dencher, N. A., Forsyth, V. T., Fragneto, G., Frick, B., Gilles, R., Gutberlet, T., Haertlein, M., Hauss, T., Haeussler, W., Heller, W. T., Herwig, K., Holderer, O., Juranyi, F., Kampmann, R., Knott, R., Krueger, S., Langan, P., Lechner, R. E., Lynn, G., Majkrzak, C., May, R. P., Meilleur, F., Mo, Y., Mortensen, Kell, Myles, D. A. A., Natali, F., Neylon, C., Niimura, N., Ollivier, J., Ostermann, A., Peters, J., Pieper, J., Ruehm, A., Schwahn, D., Shibata, K., Soper, A. K., Straessle, Th., Suzuki, J., Tanaka, I., Tehei, M., Timmins, P., Torikai, N., Unruh, T., Urban, V., Vavrin, R., Weiss, K., Teixeira, S. C. M., Zaccai, G., Ankner, J., Bellissent-Funel, M. C., Bewley, R., Blakeley, M. P., Callow, P., Coates, L., Dahint, R., Dalgliesh, R., Dencher, N. A., Forsyth, V. T., Fragneto, G., Frick, B., Gilles, R., Gutberlet, T., Haertlein, M., Hauss, T., Haeussler, W., Heller, W. T., Herwig, K., Holderer, O., Juranyi, F., Kampmann, R., Knott, R., Krueger, S., Langan, P., Lechner, R. E., Lynn, G., Majkrzak, C., May, R. P., Meilleur, F., Mo, Y., Mortensen, Kell, Myles, D. A. A., Natali, F., Neylon, C., Niimura, N., Ollivier, J., Ostermann, A., Peters, J., Pieper, J., Ruehm, A., Schwahn, D., Shibata, K., Soper, A. K., Straessle, Th., Suzuki, J., Tanaka, I., Tehei, M., Timmins, P., Torikai, N., Unruh, T., Urban, V., Vavrin, R., and Weiss, K.

Published
2008

29. New sources and instrumentation for neutrons in biology (vol 345, pg 133, 2008)

Author

Teixeira, S. C. M., Zaccai, G., Ankner, J., Bellissent-Funel, M. C., Bewley, R., Blakeley, M. P., Callow, P., Coates, L., Dahint, R., Dalgliesh, R., Dencher, N. A., Forsyth, V. T., Fragneto, G., Frick, B., Gilles, R., Gutberlet, T., Haertlein, M., Hauss, T., Haeussler, W., Heller, W. T., Herwig, K., Holderer, O., Juranyi, F., Kampmann, R., Knott, R., Krueger, S., Langan, P., Lechner, R. E., Lynn, G., Majkrzak, C., May, R. P., Meilleur, F., Mo, Y., Mortensen, Kell, Myles, D. A. A., Natali, F., Neylon, C., Niimura, N., Ollivier, J., Ostermann, A., Peters, J., Pieper, J., Ruehm, A., Schwahn, D., Shibata, K., Soper, A. K., Straessle, Th., Suzuki, J., Tanaka, I., Tehei, M., Timmins, P., Torikai, N., Unruh, T., Urban, V., Vavrin, R., Weiss, K., Teixeira, S. C. M., Zaccai, G., Ankner, J., Bellissent-Funel, M. C., Bewley, R., Blakeley, M. P., Callow, P., Coates, L., Dahint, R., Dalgliesh, R., Dencher, N. A., Forsyth, V. T., Fragneto, G., Frick, B., Gilles, R., Gutberlet, T., Haertlein, M., Hauss, T., Haeussler, W., Heller, W. T., Herwig, K., Holderer, O., Juranyi, F., Kampmann, R., Knott, R., Krueger, S., Langan, P., Lechner, R. E., Lynn, G., Majkrzak, C., May, R. P., Meilleur, F., Mo, Y., Mortensen, Kell, Myles, D. A. A., Natali, F., Neylon, C., Niimura, N., Ollivier, J., Ostermann, A., Peters, J., Pieper, J., Ruehm, A., Schwahn, D., Shibata, K., Soper, A. K., Straessle, Th., Suzuki, J., Tanaka, I., Tehei, M., Timmins, P., Torikai, N., Unruh, T., Urban, V., Vavrin, R., and Weiss, K.

Published
2008

36. Erratum to “New sources and instrumentation for neutrons in biology” [Chem. Phys. 345 (2008) 133–151]

Author

Teixeira, S.C.M., primary, Zaccai, G., additional, Ankner, J., additional, Bellissent-Funel, M.C., additional, Bewley, R., additional, Blakeley, M.P., additional, Callow, P., additional, Coates, L., additional, Dahint, R., additional, Dalgliesh, R., additional, Dencher, N.A., additional, Forsyth, V.T., additional, Fragneto, G., additional, Frick, B., additional, Gilles, R., additional, Gutberlet, T., additional, Haertlein, M., additional, Hauß, T., additional, Häußler, W., additional, Heller, W.T., additional, Herwig, K., additional, Holderer, O., additional, Juranyi, F., additional, Kampmann, R., additional, Knott, R., additional, Krueger, S., additional, Langan, P., additional, Lechner, R.E., additional, Lynn, G., additional, Majkrzak, C., additional, May, R.P., additional, Meilleur, F., additional, Mo, Y., additional, Mortensen, K., additional, Myles, D.A.A., additional, Natali, F., additional, Neylon, C., additional, Niimura, N., additional, Ollivier, J., additional, Ostermann, A., additional, Peters, J., additional, Pieper, J., additional, Rühm, A., additional, Schwahn, D., additional, Shibata, K., additional, Soper, A.K., additional, Strässle, Th., additional, Suzuki, J., additional, Tanaka, I., additional, Tehei, M., additional, Timmins, P., additional, Torikai, N., additional, Unruh, T., additional, Urban, V., additional, Vavrin, R., additional, and Weiss, K., additional

Published
2008
Full Text
View/download PDF

47. Nanobubbles and Their Precursor Layer at the Interface of Water Against a Hydrophobic Substrate

Author

Steitz, R., Gutberlet, T., Hauss, T., Klosgen, B., Krastev, R., Schemmel, S., Simonsen, A. C., and Findenegg, G. H.

Abstract

Neutron reflectivity experiments on the interface of pure D2O against thin films of perdeuterated polystyrene (d-PS) spin-coated onto silicon blocks were performed to study the intrinsic structure of the interface of water against hydrophobic substrates. The experiments reveal nonvanishing scattering contrast at the polymer/water interface, although the two materials (d-PS and D2O) have closely similar scattering length densities. Organic (nondeuterated) contaminants or macroscopic air bubbles trapped at the polymer/water interface can be ruled out as the origin of this observation. From a systematic study of this system, it is concluded that the source of the nonvanishing contrast is a depletion of water in the boundary layer against the hydrophobic surface. It is conjectured that this depletion layer represents a precursor layer of submicroscopic gas bubbles recently observed by Tyrrell and Attard. The existence of such gas nanobubbles in the present system is confirmed by atomic force microscopy (AFM) of the surface of d-PS coatings in contact with bulk water. The thickness of the precursor gas layer as determined by neutron reflectometry is 2−5 nm, depending on the level of air saturation of the water sample and on the time elapsed after contacting it with the hydrophobic surface.

Published
2003

48. Dehydration of biological membranes by cooling: an investigation on the purple membrane11Edited by J. Karn

Author

Lechner, R.E, Fitter, J, Dencher, N.A, and Hauß, T

Abstract

The lamellar spacing dlof purple membrane (PM) multilayer systems was investigated with neutron diffraction as a function of temperature and of the level of hydration. The observed large T-dependent variations of dlindicate that PM is partially dehydrated when cooled below a “hydration water freezing point”. This phenomenon is reversible, but a hysteresis is observed when PM is rehydrated upon reheating. The hydration water remaining bound to the membrane below about 240 K is non-freezing. Its amount was found to be hnf= 0.24(±0.02) g 2H2O/g BR for all samples equilibrated at room temperature in the presence of 2H2O vapour at ⩾84% r.h. It is evident, that the dehydration/rehydration behaviour of PM is strongly correlated with the temperature-dependent behaviour of the dynamical structure factor. Above the well-known “dynamical transition” announcing the onset of localized diffusive molecular motions between 190 K and 230 K, a second dynamical transition is caused by the temperature-induced rehydration of the PM starting near 255 K. This is also correlated with the deviation from a pure Arrhenius law of the rate-limiting process in the photocycle, known to occur upon cooling beyond the ice point into the same temperature region. Our results suggest that the phenomenon of dehydration and rehydration induced by cooling and reheating, respectively, is a general property of biological membranes.

Published
1998
Full Text
View/download PDF

49. Structure and hydration of the m-state of the bacteriorhodopsin mutant D96N studied by neutron diffraction11Edited by M. F. Moody

Author

Weik, M., Zaccai, G., Dencher, N.A., Oesterhelt, D., and Hauß, T.

Abstract

Neutron diffraction from oriented purple membrane fragments at various hydration levels, coupled with H2O/2H2O exchange, was used to compare the structure and hydration of the light-adapted initial state (B-state) and the M photointermediate of bacteriorhodopsin mutant D96N. Diffraction patterns were recorded at 86%, 75% and 57% relative humidity (r.h.).

Published
1998
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results