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Publicado por Springer, 2013
ISBN 10: 3642269532ISBN 13: 9783642269530
Librería: booksXpress, Bayonne, NJ, Estados Unidos de America
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Soft Cover. Condición: new. This item is printed on demand.
Publicado por Springer, 2013
ISBN 10: 3642269532ISBN 13: 9783642269530
Librería: Lucky's Textbooks, Dallas, TX, Estados Unidos de America
Libro
Condición: New.
Publicado por Springer, 2013
ISBN 10: 3642269532ISBN 13: 9783642269530
Librería: Ria Christie Collections, Uxbridge, Reino Unido
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Condición: New. PRINT ON DEMAND Book; New; Fast Shipping from the UK. No. book.
Publicado por Springer Berlin Heidelberg Sep 2011, 2011
ISBN 10: 3642225918ISBN 13: 9783642225918
Librería: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, Alemania
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Buch. Condición: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -There are nearly 100 000 different protein sequences encoded in the human genome, each with its own specific fold. Understanding how a newly formed polypeptide sequence finds its way to the correct fold is one of the greatest challenges in the modern structural biology. The aim of this thesis is to provide novel insights into protein folding by considering the problem from the point of view of statistical mechanics. The thesis starts by investigating the fundamental degrees of freedom in polypeptides that are responsible for the conformational transitions. This knowledge is then applied in the statistical mechanics description of helix coil transitions in polypeptides. Finally, the theoretical formalism is generalized to the case of proteins in an aqueous environment. The major novelty of this work lies in combining (a) a formalism based on fundamental physical properties of the system and (b) the resulting possibility of describing the folding unfolding transitions quantitatively. The clear physical nature of the formalism opens the way to further applications in a large variety of systems and processes. 136 pp. Englisch.
Publicado por Springer Berlin Heidelberg Nov 2013, 2013
ISBN 10: 3642269532ISBN 13: 9783642269530
Librería: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, Alemania
Libro Impresión bajo demanda
Taschenbuch. Condición: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -There are nearly 100 000 different protein sequences encoded in the human genome, each with its own specific fold. Understanding how a newly formed polypeptide sequence finds its way to the correct fold is one of the greatest challenges in the modern structural biology. The aim of this thesis is to provide novel insights into protein folding by considering the problem from the point of view of statistical mechanics. The thesis starts by investigating the fundamental degrees of freedom in polypeptides that are responsible for the conformational transitions. This knowledge is then applied in the statistical mechanics description of helix coil transitions in polypeptides. Finally, the theoretical formalism is generalized to the case of proteins in an aqueous environment. The major novelty of this work lies in combining (a) a formalism based on fundamental physical properties of the system and (b) the resulting possibility of describing the folding unfolding transitions quantitatively. The clear physical nature of the formalism opens the way to further applications in a large variety of systems and processes. 136 pp. Englisch.
Publicado por Springer Berlin Heidelberg, 2011
ISBN 10: 3642225918ISBN 13: 9783642225918
Librería: moluna, Greven, Alemania
Libro Impresión bajo demanda
Condición: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Nominated as an outstanding contribution by the University of Frankfurt Represents a fertile encounter between physics and life-sciences Presents the first physically motivated quantitative description of the protein folding/unfolding transi.
Publicado por Springer Berlin Heidelberg, 2013
ISBN 10: 3642269532ISBN 13: 9783642269530
Librería: moluna, Greven, Alemania
Libro Impresión bajo demanda
Condición: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Nominated as an outstanding contribution by the University of Frankfurt Represents a fertile encounter between physics and life-sciences Presents the first physically motivated quantitative description of the protein folding/unfolding transi.
Publicado por Springer Berlin Heidelberg, 2011
ISBN 10: 3642225918ISBN 13: 9783642225918
Librería: AHA-BUCH GmbH, Einbeck, Alemania
Libro
Buch. Condición: Neu. Druck auf Anfrage Neuware - Printed after ordering - There are nearly 100 000 different protein sequences encoded in the human genome, each with its own specific fold. Understanding how a newly formed polypeptide sequence finds its way to the correct fold is one of the greatest challenges in the modern structural biology. The aim of this thesis is to provide novel insights into protein folding by considering the problem from the point of view of statistical mechanics. The thesis starts by investigating the fundamental degrees of freedom in polypeptides that are responsible for the conformational transitions. This knowledge is then applied in the statistical mechanics description of helix coil transitions in polypeptides. Finally, the theoretical formalism is generalized to the case of proteins in an aqueous environment. The major novelty of this work lies in combining (a) a formalism based on fundamental physical properties of the system and (b) the resulting possibility of describing the folding unfolding transitions quantitatively. The clear physical nature of the formalism opens the way to further applications in a large variety of systems and processes.
Publicado por Springer Berlin Heidelberg, 2013
ISBN 10: 3642269532ISBN 13: 9783642269530
Librería: AHA-BUCH GmbH, Einbeck, Alemania
Libro
Taschenbuch. Condición: Neu. Druck auf Anfrage Neuware - Printed after ordering - There are nearly 100 000 different protein sequences encoded in the human genome, each with its own specific fold. Understanding how a newly formed polypeptide sequence finds its way to the correct fold is one of the greatest challenges in the modern structural biology. The aim of this thesis is to provide novel insights into protein folding by considering the problem from the point of view of statistical mechanics. The thesis starts by investigating the fundamental degrees of freedom in polypeptides that are responsible for the conformational transitions. This knowledge is then applied in the statistical mechanics description of helix coil transitions in polypeptides. Finally, the theoretical formalism is generalized to the case of proteins in an aqueous environment. The major novelty of this work lies in combining (a) a formalism based on fundamental physical properties of the system and (b) the resulting possibility of describing the folding unfolding transitions quantitatively. The clear physical nature of the formalism opens the way to further applications in a large variety of systems and processes.
Publicado por Springer Verlag, 2013
ISBN 10: 3642269532ISBN 13: 9783642269530
Librería: Revaluation Books, Exeter, Reino Unido
Libro
Paperback. Condición: Brand New. 2011 edition. 160 pages. 9.25x6.10x0.32 inches. In Stock.
Publicado por Springer, 2011
ISBN 10: 3642225918ISBN 13: 9783642225918
Librería: Mispah books, Redhill, SURRE, Reino Unido
Libro
Hardcover. Condición: Like New. Like New. book.
Publicado por Springer, 2013
ISBN 10: 3642269532ISBN 13: 9783642269530
Librería: Mispah books, Redhill, SURRE, Reino Unido
Libro
Paperback. Condición: Like New. Like New. book.
Publicado por Springer-Verlag Berlin and Heidelberg GmbH & Co. KG, Berlin, 2011
ISBN 10: 3642225918ISBN 13: 9783642225918
Librería: CitiRetail, Stevenage, Reino Unido
Libro
Hardcover. Condición: new. Hardcover. There are nearly 100 000 different protein sequences encoded in the human genome, each with its own specific fold. Understanding how a newly formed polypeptide sequence finds its way to the correct fold is one of the greatest challenges in the modern structural biology. The aim of this thesis is to provide novel insights into protein folding by considering the problem from the point of view of statistical mechanics. The thesis starts by investigating the fundamental degrees of freedom in polypeptides that are responsible for the conformational transitions. This knowledge is then applied in the statistical mechanics description of helix coil transitions in polypeptides. Finally, the theoretical formalism is generalized to the case of proteins in an aqueous environment. The major novelty of this work lies in combining (a) a formalism based on fundamental physical properties of the system and (b) the resulting possibility of describing the folding unfolding transitions quantitatively. The clear physical nature of the formalism opens the way to further applications in a large variety of systems and processes. This thesis provides novel insights into protein folding by considering the problem from the point of view of statistical mechanics. It presents the first physically motivated quantitative description of the protein folding/unfolding transition. Shipping may be from our UK warehouse or from our Australian or US warehouses, depending on stock availability.