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This edited volume discusses the identification, discovery, characterization, structure determination and modeling of multicomponent macromolecular complexes, and as such, it fully complements the first volume (ISBN 978-3-319-27214-6), which targeted methods of recombinant production of protein complexes. This book is divided in 8 sections offering a selection of technologies widely used in the characterization of protein and protein-nucleic acid complexes for different purposes and at different scales. From native electrophoresis methods, that are accessible to any reasonably well-equipped laboratory, to the sophisticated setup required for structure determination by cryo-electron microscopy or X-ray crystallography, this book contains a wide variety of clearly explained analytic and preparative approaches, connected with the production techniques developed on the previous volume. The readers will find an integral connection between this book and the first volume, which ensures a comprehensive and updated discussion of the main topics of the discipline. Taken together, these volumes constitute a cohesive and authoritative source of the research on multicomponent macromolecular complexes. In here, we focus on characterization of protein complexes in the broadest sense, which is not typically covered in other sources. Moreover, all chapters are carefully written by world renowned scientists and active researchers, making this volume ideal, not only as a reference source, but also as a companion book for the daily laboratory work. This book is aimed for a wide range of scientists, from science students to experienced researchers, working on protein and protein-nucleic acid complexes, who need a thorough understanding of protein production and complex characterization. .

Life sciences. --- Life Sciences.

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This book compiles research on Enterobacterales characterization concerning the presence of genes associated with virulence (adhesins; surface cellulose structures and curli; siderophores, e.g., enterobactin, aerobactin, and yersiniabactin; protectines; invasins or toxins), and, furthermore, bacterial-biofilm-associated phenotypes. Although not directly involved in pathogenicity, the acquisition of multiple antibiotic resistances strongly supports the success of opportunistic Enterobacterales pathogens in invasion, survival, and spread and markedly complicates the treatment of infections. Not only pathogens, but also commensal bacteria, considered harmless and part of the normal microbiota, are exposed to selection pressure and can be a reservoir of mobile genetic elements carrying antibiotic resistance genes. Therefore, the occurrence of drug-resistant bacteria within a commensal population and the possibility to exchange genetic material through horizontal gene transfer may represent a major health concern.

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There is considerable interest today for the reactions of anticancer metallodrugs with proteins as these interactions might feature processes that are crucial for the biodistribution, the toxicity and even the mechanism of action of this important group of anticancer agents. Valuable structural and functional information on these adducts could be derived from several biophysical studies mainly relying on the application of X-ray diffraction and ESI MS techniques. The structural and functional information achieved on the respective metallodrug-protein adducts allowed us to identify some general trends in the reactivity of anticancer metallodrugs with protein targets.

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Population dynamics constitutes a widespread branch of investigations which finds important applications within the realm of life science. The classical deterministic (macroscopic) approach aims at characterizing the time evolution of families of homologous entities, so to unravel the global mechanisms which drive their dynamics. As opposed to this formulation, a microscopic level of modeling can be invoked which instead focuses on the explicit rules governing the interactions among individuals. A viable tool that enables to bridge the gap between the two approaches is the van Kampen's system size expansion. In this thesis we use this method to show how the finite-size effects accounted by the microscopic level might significantly alter the dynamics of biological phenomena.

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In humans, ascorbic acid is an essential vitamin, anti-oxidant and co-factor of a variety of metal ion-dependent enzymatic reactions. In this review, the transport of L-ascorbic acid is described from food to target cells. Transport of ascorbic acid across the plasma membrane is facilitated by members of the SLC23 family, SLC23A1/SVCT1 and SLC23A2/SVCT2. We present in silico models of these transporters that provide new insights into the structure of the SLC23 family. While SVCT1 is mainly responsible for uptake of ascorbic acid from the intestine into the blood and for reabsorption in the kidney, the more broadly expressed transporter SVCT2 delivers ascorbic acid into tissues that are in high demand of the vitamin. The oxidized form of ascorbic acid, dehydroascorbic acid (DHA), is a substrate of the GLUT transporters belonging to the SLC2 family. They play important roles in ascorbic acid recycling, such as in the brain and in erythrocytes. Ascorbic acid serves as an essential co-factor of metal ion-dependent enzymes, keeping their metal ions in the reduced state. In addition, it serves as an effective antioxidant in cells with high metabolic activity such as neurons. Thus, it is not too surprising that changes in expression and function of the SVCTs have nutritional and pathological consequences such as during ageing, malnutrition and chronic alcohol abuse or in cancer, neurodegenerative diseases and chronic inflammation diseases. In the future, SVCT1 and SVCT2 may furthermore prove useful as drug delivery systems, to enhance transport of novel pharmaceutical agents more efficiently across the intestinal epithelium and the blood-cerebrospinal fluid barrier.

Life sciences.