This book presents a new view of the mechanism of functional expression of ATP-driven motors (proteins or protein complexes). It is substantially different from the prevailing idea that the motor converts chemical energy to mechanical work. To facilitate understanding, the differences between the new and prevailing views are explained using many illustrations. The book is of interest to those who are not convinced of the notion of chemo–mechanical coupling. The claims presented are the following: The system, which comprises not only the motor but also water, does no mechanical work during the ATP hydrolysis cycle; a protein is moved or a protein in the complex is rotated by the entropic force generated by water. The highlight of the explanation in the book is that the mechanism of unidirectional rotation of the central shaft in F1-ATPase is discussed in detail on the basis of this new view. The hydration entropy of each ß subunit to which a specific chemical compound (ATP, ADP and Pi, Pi, or nothing) is bound, the hydration entropy of the a3ß3 complex, and the dependence of the hydration entropy of F1-ATPase on the orientation of the ? subunit play essential roles.
Le informazioni nella sezione "Riassunto" possono far riferimento a edizioni diverse di questo titolo.
Masahiro Kinoshita received his Doctor of Engineering degree from Kyoto University in 1984. His research interests include statistical–mechanical theories of fluids (integral equation theories), hydrophobic hydration, unified elucidation of a variety of biological self-assembly processes, protein folding and unfolding, molecular recognition, mechanism of functional expression of ATP-driven motors, and thermostabilization of membrane proteins. He is currently a professor emeritus at Kyoto University and an invited researcher at Chiba University.
He has published 211 articles in internationally renowned journals such as Nature Chemical Biology, Journal of the American Chemical Society, and Physical Review Letters, to mention just a few. In addition, he has authored or made valuable contributions to several books in his field.
This book presents a new view of the mechanism of functional expression of ATP-driven motors (proteins or protein complexes). It is substantially different from the prevailing idea that the motor converts chemical energy to mechanical work. To facilitate understanding, the differences between the new and prevailing views are explained using many illustrations. The book is of interest to those who are not convinced of the notion of chemo–mechanical coupling. The claims presented are the following: The system, which comprises not only the motor but also water, does no mechanical work during the ATP hydrolysis cycle; a protein is moved or a protein in the complex is rotated by the entropic force generated by water. The highlight of the explanation in the book is that the mechanism of unidirectional rotation of the central shaft in F1-ATPase is discussed in detail on the basis of this new view. The hydration entropy of each ß subunit to which a specific chemical compound (ATP, ADP and Pi, Pi, or nothing) is bound, the hydration entropy of the a3ß3 complex, and the dependence of the hydration entropy of F1-ATPase on the orientation of the ? subunit play essential roles.
Le informazioni nella sezione "Su questo libro" possono far riferimento a edizioni diverse di questo titolo.
EUR 17,06 per la spedizione da U.S.A. a Italia
Destinazione, tempi e costiEUR 9,70 per la spedizione da Germania a Italia
Destinazione, tempi e costiDa: moluna, Greven, Germania
Kartoniert / Broschiert. Condizione: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Presents a new view of the mechanism of functional expression of ATP-driven motorsElucidates four cases on the rotation of the central shaft in F1-ATPase in a unified theoryExplains ideas i. Codice articolo 449943435
Quantità: Più di 20 disponibili
Da: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, Germania
Taschenbuch. Condizione: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -This book presents a new view of the mechanism of functional expression of ATP-driven motors (proteins or protein complexes). It is substantially different from the prevailing idea that the motor converts chemical energy to mechanical work. To facilitate understanding, the differences between the new and prevailing views are explained using many illustrations. The book is of interest to those who are not convinced of the notion of chemo-mechanical coupling. The claims presented are the following: The system, which comprises not only the motor but also water, does no mechanical work during the ATP hydrolysis cycle; a protein is moved or a protein in the complex is rotated by the entropic force generated by water. The highlight of the explanation in the book is that the mechanism of unidirectional rotation of the central shaft in F1-ATPase is discussed in detail on the basis of this new view. The hydration entropy of each beta subunit to which a specific chemical compound (ATP, ADP and Pi, Pi, or nothing) is bound, the hydration entropy of the 3beta3complex, and the dependence of the hydration entropy of F1-ATPase on the orientation of the Gamma subunit play essential roles. 92 pp. Englisch. Codice articolo 9789813362345
Quantità: 2 disponibili
Da: buchversandmimpf2000, Emtmannsberg, BAYE, Germania
Taschenbuch. Condizione: Neu. Neuware -This book presents a new view of the mechanism of functional expression of ATP-driven motors (proteins or protein complexes). It is substantially different from the prevailing idea that the motor converts chemical energy to mechanical work. To facilitate understanding, the differences between the new and prevailing views are explained using many illustrations. The book is of interest to those who are not convinced of the notion of chemömechanical coupling. The claims presented are the following: The system, which comprises not only the motor but also water, does no mechanical work during the ATP hydrolysis cycle; a protein is moved or a protein in the complex is rotated by the entropic force generated by water. The highlight of the explanation in the book is that the mechanism of unidirectional rotation of the central shaft in F1-ATPase is discussed in detail on the basis of this new view. The hydration entropy of each ¿ subunit to which a specific chemical compound (ATP, ADP and Pi, Pi, or nothing) is bound, the hydration entropy of the ¿3¿3 complex, and the dependence of the hydration entropy of F1-ATPase on the orientation of the ¿ subunit play essential roles.Springer Verlag GmbH, Tiergartenstr. 17, 69121 Heidelberg 92 pp. Englisch. Codice articolo 9789813362345
Quantità: 2 disponibili
Da: Ria Christie Collections, Uxbridge, Regno Unito
Condizione: New. In. Codice articolo ria9789813362345_new
Quantità: Più di 20 disponibili
Da: GreatBookPrices, Columbia, MD, U.S.A.
Condizione: New. Codice articolo 43625023-n
Quantità: Più di 20 disponibili
Da: California Books, Miami, FL, U.S.A.
Condizione: New. Codice articolo I-9789813362345
Quantità: Più di 20 disponibili
Da: AHA-BUCH GmbH, Einbeck, Germania
Taschenbuch. Condizione: Neu. Druck auf Anfrage Neuware - Printed after ordering - This book presents a new view of the mechanism of functional expression of ATP-driven motors (proteins or protein complexes). It is substantially different from the prevailing idea that the motor converts chemical energy to mechanical work. To facilitate understanding, the differences between the new and prevailing views are explained using many illustrations. The book is of interest to those who are not convinced of the notion of chemo-mechanical coupling. The claims presented are the following: The system, which comprises not only the motor but also water, does no mechanical work during the ATP hydrolysis cycle; a protein is moved or a protein in the complex is rotated by the entropic force generated by water. The highlight of the explanation in the book is that the mechanism of unidirectional rotation of the central shaft in F1-ATPase is discussed in detail on the basis of this new view. The hydration entropy of each beta subunit to which a specific chemical compound (ATP, ADP and Pi, Pi, or nothing) is bound, the hydration entropy of the 3beta3complex, and the dependence of the hydration entropy of F1-ATPase on the orientation of the Gamma subunit play essential roles. Codice articolo 9789813362345
Quantità: 1 disponibili
Da: Best Price, Torrance, CA, U.S.A.
Condizione: New. SUPER FAST SHIPPING. Codice articolo 9789813362345
Quantità: 2 disponibili
Da: GreatBookPricesUK, Woodford Green, Regno Unito
Condizione: New. Codice articolo 43625023-n
Quantità: Più di 20 disponibili
Da: GreatBookPrices, Columbia, MD, U.S.A.
Condizione: As New. Unread book in perfect condition. Codice articolo 43625023
Quantità: Più di 20 disponibili