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Añadir al carritoBuch. Condición: Neu. Druck auf Anfrage Neuware - Printed after ordering - When I was invited to edit this volume, I wanted to take the opportunity to assemble reviews of different biophysical methodologies for protein interactions at a level suf ciently detailed to understand how complex systems can be studied. There are several excellent introductory texts for biophysical methodologies, many with hands-on descriptions or embedded in general introductions to physical b- chemistry. The goal of the present volume was to present state-of-the-art reviews that do not necessarily enable the reader to carry out these techniques, but to gain a deep understanding of the biophysical observables, to stimulate creative thought on how the techniques may be applied to study a particular biological system, and to foster collaboration and multidisciplinary work. Reversible protein interactions involve noncovalent chemical bonds, pro- cing protein complexes with free energies not far from the order of magnitude of the thermal energy kT. As a consequence, they can be highly dynamic and may be controlled, for example, by protein expression levels and changes in the intracel- lar or microenvironment. Reversible protein complexes may have suf cient stab- ity to be puri ed for study, but frequently their short lifetime essentially limits their existence to solutions of mixtures of the binding partners in which they remain populated through dissociation and reassociation processes. To understand the function of such protein complexes, it is important to study their structure and dynamics.
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Publicado por SP SPRINGER, 2007
ISBN 10: 0387359656 ISBN 13: 9780387359656
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Añadir al carritoCondición: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Examines how biophysical approaches can be used to study complex systems of reversibly interacting proteins and shows how to synergistically incorporate several methodologies for useCovers calorimetry, fluorescence, surface plasmon resonance, evan.
Librería: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, Alemania
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Añadir al carritoBuch. Condición: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -This volume successfully and clearly examines how biophysical approaches can be used to study complex systems of reversibly interacting proteins. It deals with the methodology behind the research and shows how to synergistically incorporate several methodologies for use. Each chapter treats and introduces the reader to different biological systems, includes a brief summary of the physical principles, and mentions practical requirements. 548 pp. Englisch.
Idioma: Inglés
Publicado por Springer US, Humana Apr 2007, 2007
ISBN 10: 0387359656 ISBN 13: 9780387359656
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Añadir al carritoBuch. Condición: Neu. This item is printed on demand - Print on Demand Titel. Neuware -When I was invited to edit this volume, I wanted to take the opportunity to assemble reviews of different biophysical methodologies for protein interactions at a level suf ciently detailed to understand how complex systems can be studied. There are several excellent introductory texts for biophysical methodologies, many with hands-on descriptions or embedded in general introductions to physical b- chemistry. The goal of the present volume was to present state-of-the-art reviews that do not necessarily enable the reader to carry out these techniques, but to gain a deep understanding of the biophysical observables, to stimulate creative thought on how the techniques may be applied to study a particular biological system, and to foster collaboration and multidisciplinary work. Reversible protein interactions involve noncovalent chemical bonds, pro- cing protein complexes with free energies not far from the order of magnitude of the thermal energy kT. As a consequence, they can be highly dynamic and may be controlled, for example, by protein expression levels and changes in the intracel- lar or microenvironment. Reversible protein complexes may have suf cient stab- ity to be puri ed for study, but frequently their short lifetime essentially limits their existence to solutions of mixtures of the binding partners in which they remain populated through dissociation and reassociation processes. To understand the function of such protein complexes, it is important to study their structure and dynamics.Springer-Verlag GmbH, Tiergartenstr. 17, 69121 Heidelberg 548 pp. Englisch.