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Your search keyword '"Petra Born"' showing total 3 results
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3 results on '"Petra Born"'

1. List of Contributors

Author

Nawaf Al-Maharik, Heidi Annuk, Michael A. Apicella, Ben J. Appelmelk, Ivo G. Boneca, Petra Born, Klaus Brandenburg, Patrick J. Brennan, Volker Briken, Eric D. Brown, Stephen D. Carrington, Paola Cescutti, Delphi Chatterjee, Marguerite Clyne, Richard M. Cooper, Anthony P. Corfield, Monica M. Cunneen, Piet W.J. de Groot, Gennaro De Libero, Clara G. de los Reyes-Gavilán, Tamara L. Doering, Max Dow, Nicole N. Driessen, Jeffrey C. Dyason, Eva Maria Egelseer, Alan D. Elbein, Mario F. Feldman, Eamonn Fitz Patrick, Yukari Fujimoto, Koichi Fukase, Patrick Garidel, Jeroen Geurtsen, Marlyn Gonzalez, I. Darren Grice, Patricia Guerry, Thomas Gutsmann, Holger Heine, Joanne Heng, Otto Holst, Harold. J Jennings, Michael P. Jennings, Margaret I. Kanipes, Dennis L. Kasper, Wafa Khamri, Milton J. Kiefel, Dionne C.G. Klein, Frans M. Klis, Yuriy A. Knirel, Thomas Kohler, Paul Kosma, Emir Kulauzovic, Shoichi Kusumoto, John R. Lawrence, Clifford A. Lingwood, Peter N. Lipke, Susan M. Logan, Radia Mahfoud, Malcolm J. McConville, Rachel M. McLoughlin, Paul Messner, Antonio Molinaro, Anthony P. Moran, Thomas Naderer, Thomas R. Neu, Mari-Anne Newman, Andrei V. Nikolaev, Christian M. Pedersen, Mark P. Pereira, Andreas Peschel, Stefan Pöhlmann, Robert A. Pon, Stuart A. Ralph, Peter R. Reeves, Anne N. Reid, Colm J. Reid, Morgann C. Reilly, Sabine Riekenberg, Patricia Ruas-Madiedo, Nuria Salazar, Christina Schäffer, Richard R. Schmidt, Ian C. Schoenhofen, Marit Sletmoen, Uwe B. Sleytr, Evelyn C. Soo, Imke Steffen, Daniel C. Stein, Bjørn T. Stokke, Christine M. Szymanski, Joe Tiralongo, Jennifer A. Tee, Mark R. Thursz, M. Stephen Trent, Theodros S. Tsegaye, Jean van Heijenoort, Waldemar Vollmer, Mark von Itzstein, Jennifer C. Wilson, and Guoqing Xia

Published
2010
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2. Bacterial cell envelope peptidoglycan

Author

Waldemar Vollmer and Petra Born

Subjects
Glycan, Pseudopeptidoglycan, Sequence (biology), Biology, biology.organism_classification, Bacterial cell structure, carbohydrates (lipids), chemistry.chemical_compound, Biochemistry, chemistry, biology.protein, Peptidoglycan, Cell envelope, Peptide sequence, Bacteria
Abstract

Publisher Summary This chapter provides an overview on the diversity and variability of the peptidoglycan structures found in various bacteria. It summarizes the biophysical properties of peptidoglycan and discusses its architecture. Peptidoglycan is responsible for the osmotic stability by encasing the cytoplasmic membrane of most bacteria. It is a unique, net-like polymer made of glycan strands that are cross-linked by unusual peptides. Although there are some common structural features of peptidoglycan, there is large variability in the structure of bacterial peptidoglycan due to differences in the amino acid sequence, types of cross-links, and the presence or absence of secondary modifications in both the glycan strands and peptides. The glycans are synthesized as oligo- ( N -acetylglucosamine- N -acetylmuramic acid) strands of variable length and become modified shortly after their synthesis in many species. The peptides contain L- and D-amino acids and have a species-specific amino acid composition, sequence, and type of cross-linkage. Maturation of peptidoglycan involves cleavage of amide bonds in the peptides resulting in a nonhomogeneous structure of the polymer. Introduction of secondary modifications and maturation are the reasons for the complex composition of mature peptidoglycan often manifesting in a species-specific fine structure.

Published
2010
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3. A spatially hybrid fluid-kinetic neutral model for SOLPS-ITER plasma edge simulations

Author

Maarten Blommaert, Niels Horsten, Petra Börner, and Wouter Dekeyser

Subjects
Nuclear engineering. Atomic power, TK9001-9401
Abstract

Plasma edge transport simulations typically rely on Monte-Carlo simulations for the kinetic neutral transport. However, for detached operating conditions the dominance of charge-exchange reactions between plasma and neutrals leads to excessive computational costs of these Monte-Carlo simulations. Since the fluid assumption becomes valid in these highly-collisional conditions, the use of a fluid neutral model is interesting to reduce computational costs. In this paper, we show within the SOLPS-ITER code suite that while our recently developed fluid neutral model is able to accurately represent the neutral transport in the divertor, it is unable to capture the kinetic effects near the outer wall. Due to this model flaw, discrepancies in plasma state arise between the fluid plasma-neutral model and a simulation with kinetic neutrals after converging the model equations. As a solution, we present a spatially hybrid neutral model that captures these kinetic effects near the wall, while benefiting from the fluid approach in the divertor region. Moreover, by using the kinetic code in the region outside the plasma grid, the method is able to accurately account for neutral transport through the voids surrounding the plasma and into pumps. We show on a case with a simplified ‘slab’ geometry that the results of the proposed hybrid model compare excellently to those of the kinetic solution. Keywords: Plasma edge simulation, Hybrid fluid-kinetic neutral model

Published
2019
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