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Edité par Springer, 2013
ISBN 10 : 3642269532ISBN 13 : 9783642269530
Vendeur : booksXpress, Bayonne, NJ, Etats-Unis
Livre impression à la demande
Soft Cover. Etat : new. This item is printed on demand.
Edité par Springer, 2011
ISBN 10 : 3642688934ISBN 13 : 9783642688935
Vendeur : booksXpress, Bayonne, NJ, Etats-Unis
Livre impression à la demande
Soft Cover. Etat : new. This item is printed on demand.
Edité par Springer, 2013
ISBN 10 : 3642269532ISBN 13 : 9783642269530
Vendeur : Lucky's Textbooks, Dallas, TX, Etats-Unis
Livre
Etat : New.
Edité par Springer, 2013
ISBN 10 : 3642269532ISBN 13 : 9783642269530
Vendeur : Ria Christie Collections, Uxbridge, Royaume-Uni
Livre impression à la demande
Etat : New. PRINT ON DEMAND Book; New; Fast Shipping from the UK. No. book.
Edité par Springer Berlin Heidelberg Sep 2011, 2011
ISBN 10 : 3642225918ISBN 13 : 9783642225918
Vendeur : BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, Allemagne
Livre impression à la demande
Buch. Etat : 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.
Edité par Springer Berlin Heidelberg Nov 2013, 2013
ISBN 10 : 3642269532ISBN 13 : 9783642269530
Vendeur : BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, Allemagne
Livre impression à la demande
Taschenbuch. Etat : 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.
Edité par Springer Berlin Heidelberg, 2011
ISBN 10 : 3642225918ISBN 13 : 9783642225918
Vendeur : moluna, Greven, Allemagne
Livre impression à la demande
Etat : 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.
Edité par Springer Berlin Heidelberg, 2013
ISBN 10 : 3642269532ISBN 13 : 9783642269530
Vendeur : moluna, Greven, Allemagne
Livre impression à la demande
Etat : 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.
Edité par Springer Berlin Heidelberg, 2011
ISBN 10 : 3642225918ISBN 13 : 9783642225918
Vendeur : AHA-BUCH GmbH, Einbeck, Allemagne
Livre
Buch. Etat : 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.
Edité par Springer Berlin Heidelberg, 2013
ISBN 10 : 3642269532ISBN 13 : 9783642269530
Vendeur : AHA-BUCH GmbH, Einbeck, Allemagne
Livre
Taschenbuch. Etat : 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.
Edité par Springer Verlag, 2013
ISBN 10 : 3642269532ISBN 13 : 9783642269530
Vendeur : Revaluation Books, Exeter, Royaume-Uni
Livre
Paperback. Etat : Brand New. 2011 edition. 160 pages. 9.25x6.10x0.32 inches. In Stock.
Edité par Springer, 2011
ISBN 10 : 3642225918ISBN 13 : 9783642225918
Vendeur : Mispah books, Redhill, SURRE, Royaume-Uni
Livre
Hardcover. Etat : Like New. Like New. book.
Edité par Springer, 2013
ISBN 10 : 3642269532ISBN 13 : 9783642269530
Vendeur : Mispah books, Redhill, SURRE, Royaume-Uni
Livre
Paperback. Etat : Like New. Like New. book.
Edité par Springer-Verlag Berlin and Heidelberg GmbH & Co. KG, Berlin, 2011
ISBN 10 : 3642225918ISBN 13 : 9783642225918
Vendeur : CitiRetail, Stevenage, Royaume-Uni
Livre
Hardcover. Etat : 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.