M
Monika Schneider
Researcher at Max Planck Society
Publications - 11
Citations - 1771
Monika Schneider is an academic researcher from Max Planck Society. The author has contributed to research in topics: Random hexamer & Protein structure. The author has an hindex of 10, co-authored 11 publications receiving 1738 citations.
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Journal ArticleDOI
Crystal Structure of the Xanthine Oxidase-Related Aldehyde Oxido-Reductase from D. gigas
Maria João Romão,Margarida Archer,Isabel Moura,José J. G. Moura,Jean LeGall,Richard A. Engh,Monika Schneider,Peter Hof,Robert Huber +8 more
TL;DR: The crystal structure of the aldehyde oxido-reductase (Mop) from the sulfate reducing anaerobic Gram-negative bacterium Desulfovibrio gigas has been determined at 2.25 Å resolution by multiple isomorphous replacement and refined.
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Crystal structure analysis and refinement at 2·5 Å of hexameric C-phycocyanin from the cyanobacterium Agmenellum quadruplicatum: The molecular model and its implications for light-harvesting
TL;DR: The crystal structure of the light-harvesting protein-pigment complex C-phycocyanin from the cyanobacterium Agmenellum quadruplicatum has been determined by Patterson search techniques on the basis of the molecular model of C-PHYCOCYCLYIN from Mastigocladus laminosus as mentioned in this paper.
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Crystal and molecular structure of human annexin V after refinement. Implications for structure, membrane binding and ion channel formation of the annexin family of proteins.
Robert Huber,Robert Berendes,Alexander Burger,Monika Schneider,Andrej Karshikov,Hartmut Luecke,Jürgen Römisch,Eric Paques +7 more
TL;DR: It is suggested that annexins bind with their convex face to membranes, causing local disorder and permeability of the phospholipid bilayers.
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The calcium binding sites in human annexin V by crystal structure analysis at 2.0 A resolution. Implications for membrane binding and calcium channel activity.
TL;DR: The structural features suggest that annexin V attaches with its convex face to membranes by specified calcium mediated interactions with at least three phospholipids, and the adjacent membrane bilayer may thus become locally disordered and permeable to allow calcium inflow through the central polar channel of the molecule.
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Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 Å resolution
Robert Huber,Monika Schneider,Irmgard Mayr,Rudi Müller,Rainer Deutzmann,Franz Suter,Herbert Zuber,Heinz Falk,Hartmut Kayser +8 more
TL;DR: The bilin binding protein from the insect Pieris brassicae has been analysed for amino acid sequence, spectral properties and three-dimensional structure and the fold of BBP is related to retinol binding protein (RBP), as had been recognized in the preliminary analysis.