Merz kenneth m (43 risultati)
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Da: Ammareal, Morangis, FranciaAmmareal
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Hardcover. Condizione: Très bon. Ancien livre de bibliothèque avec équipements. Edition 1994. Ammareal reverse jusqu'à 15% du prix net de cet article à des organisations caritatives. ENGLISH DESCRIPTION Book Condition: Used, Very good. Former library book. Edition 1994. Ammareal gives back up to 15% of this item's net price to c…harity organizations.
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Paperback. Condizione: Brand New. 284 pages. 9.00x6.00x0.57 inches. In Stock.
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Da: Kennys Bookshop and Art Galleries Ltd., Galway, GY, IrlandaKennys Bookshop and Art Galleries Ltd.
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EUR 132,39
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Condizione: New. 2012. Softcover reprint of the original 1st ed. 1994. paperback. . . . . .
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Condizione: New. 2012. Paperback. . . . . .
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Da: Books Puddle, New York, NY, U.S.A.Books Puddle
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Condizione: New. pp. 596.
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Condizione: New. pp. 612.
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Da: California Books, Miami, FL, U.S.A.California Books
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Da: Ria Christie Collections, Uxbridge, Regno UnitoRia Christie Collections
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Da: preigu, Osnabrück, Germaniapreigu
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Taschenbuch. Condizione: Neu. The Protein Folding Problem and Tertiary Structure Prediction | Kenneth M. Jr. Merz (u. a.) | Taschenbuch | 581 S. | Englisch | 2012 | Birkhäuser | EAN 9781468468335 | Verantwortliche Person für die EU: Springer Basel AG in Springer Science + Business Media, Heidelberger Platz 3, 14197 Berlin, juerg…en[dot]hartmann[at]springer[dot]com | Anbieter: preigu.
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Da: Revaluation Books, Exeter, Regno UnitoRevaluation Books
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EUR 156,81
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Paperback. Condizione: Brand New. reprint edition. 500 pages. 9.25x6.10x1.30 inches. In Stock.
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Da: Kennys Bookstore, Olney, MD, U.S.A.Kennys Bookstore
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EUR 164,77
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Condizione: New. 2012. Softcover reprint of the original 1st ed. 1994. paperback. . . . . . Books ship from the US and Ireland.
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Da: Kennys Bookstore, Olney, MD, U.S.A.Kennys Bookstore
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Condizione: New. 2012. Paperback. . . . . . Books ship from the US and Ireland.
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Da: AHA-BUCH GmbH, Einbeck, GermaniaAHA-BUCH GmbH
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EUR 106,99
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Taschenbuch. Condizione: Neu. Druck auf Anfrage Neuware - Printed after ordering - A solution to the protein folding problem has eluded researchers for more than 30 years. The stakes are high. Such a solution will make 40,000 more tertiary structures available for immediate study by translating the DNA sequence information in th…e sequence databases into three-dimensional protein structures. This translation will be indispensable for the analy sis of results from the Human Genome Project, de novo protein design, and many other areas of biotechnological research. Finally, an in-depth study of the rules of protein folding should provide vital clues to the protein fold ing process. The search for these rules is therefore an important objective for theoretical molecular biology. Both experimental and theoretical ap proaches have been used in the search for a solution, with many promising results but no general solution. In recent years, there has been an exponen tial increase in the power of computers. This has triggered an incredible outburst of theoretical approaches to solving the protein folding problem ranging from molecular dynamics-based studies of proteins in solution to the actual prediction of protein structures from first principles. This volume attempts to present a concise overview of these advances. Adrian Roitberg and Ron Elber describe the locally enhanced sam pling/simulated annealing conformational search algorithm (Chapter 1), which is potentially useful for the rapid conformational search of larger molecular systems.
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Da: AHA-BUCH GmbH, Einbeck, GermaniaAHA-BUCH GmbH
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EUR 114,36
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Taschenbuch. Condizione: Neu. Druck auf Anfrage Neuware - Printed after ordering - The interface between a living cell and the surrounding world plays a critical role in numerous complex biological processes. Sperm/egg fusion, virus/cell fusion, exocytosis, endocytosis, and ion permeation are a few examples of processes involvin…g membranes. In recent years, powerful tools such as X-ray crystal lography, electron microscopy, nuclear magnetic resonance, and infra-red and Raman spectroscopy have been developed to characterize the structure and dy namics of biomembranes. Despite this progress, many of the factors responsible for the function of biomembranes are still not well understood. The membrane is a very complicated supramolecular liquid-crystalline structure that is largely composed of lipids, forming a bilayer, to which proteins and other biomolecules are anchored. Often, the lipid bilayer environment is pictured as a hydropho bic structureless slab providing a thermodynamic driving force to partition the amino acids of a membrane protein according to their solubility. However, much of the molecular complexity of the phospholipid bilayer environment is ignored in such a simplified view. It is likely that the atomic details of the polar head group region and the transition from the bulk water to the hydrophobic core of the membrane are important. An understanding of the factors responsible for the function of biomembranes thus requires a better characterization at the molec ular level of how proteins interact with lipid molecules, of how lipids affect protein structure and of how lipid molecules might regulate protein function.
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Da: Buchpark, Trebbin, GermaniaBuchpark
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EUR 82,98
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Condizione: Sehr gut. Zustand: Sehr gut | Seiten: 612 | Sprache: Englisch | Produktart: Bücher | The interface between a living cell and the surrounding world plays a critical role in numerous complex biological processes. Sperm/egg fusion, virus/cell fusion, exocytosis, endocytosis, and ion permeation are a few examples of proc…esses involving membranes. In recent years, powerful tools such as X-ray crystal lography, electron microscopy, nuclear magnetic resonance, and infra-red and Raman spectroscopy have been developed to characterize the structure and dy namics of biomembranes. Despite this progress, many of the factors responsible for the function of biomembranes are still not well understood. The membrane is a very complicated supramolecular liquid-crystalline structure that is largely composed of lipids, forming a bilayer, to which proteins and other biomolecules are anchored. Often, the lipid bilayer environment is pictured as a hydropho bic structureless slab providing a thermodynamic driving force to partition the amino acids of a membrane protein according to their solubility. However, much of the molecular complexity of the phospholipid bilayer environment is ignored in such a simplified view. It is likely that the atomic details of the polar head group region and the transition from the bulk water to the hydrophobic core of the membrane are important. An understanding of the factors responsible for the function of biomembranes thus requires a better characterization at the molec ular level of how proteins interact with lipid molecules, of how lipids affect protein structure and of how lipid molecules might regulate protein function.
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Da: Books Puddle, New York, NY, U.S.A.Books Puddle
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Condizione: New. pp. x + 274.
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Da: Mispah books, Redhill, SURRE, Regno UnitoMispah books
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Paperback. Condizione: Like New. LIKE NEW. SHIPS FROM MULTIPLE LOCATIONS. book.
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Paperback. Condizione: Like New. LIKE NEW. SHIPS FROM MULTIPLE LOCATIONS. book.
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Da: BUCHSERVICE / ANTIQUARIAT Lars Lutzer, Wahlstedt, GermaniaBUCHSERVICE / ANTIQUARIAT Lars Lutzer
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Condizione: gut. Biological Membranes: A Molecular Perspective from Computation and Experiment In englischer Sprache. pages.
Drug Design: Structure and Ligand-based Approaches
Merz, Kenneth M. (Editor)/ Ringe, Dagmar (Editor)/ Reynolds, Charles H. (Editor)
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Da: Revaluation Books, Exeter, Regno UnitoRevaluation Books
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Hardcover. Condizione: Brand New. 1st edition. 274 pages. 11.00x8.50x0.75 inches. In Stock.
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Da: Kennys Bookstore, Olney, MD, U.S.A.Kennys Bookstore
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Condizione: New. This book provides a complete snapshot of various experimental approaches to structure-based and ligand-based drug design and is illustrated with more than 200 images. Editor(s): Merz, Kenneth M., Jr., PhD; Ringe, Dagmar; Reynolds, Charles H. Num Pages: 286 pages, 204 b/w illus. 26 tables. BIC Classification: MM…G. Category: (P) Professional & Vocational. Dimension: 279 x 215 x 18. Weight in Grams: 1210. . 2010. Illustrated. hardcover. . . . . Books ship from the US and Ireland.
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Da: AHA-BUCH GmbH, Einbeck, GermaniaAHA-BUCH GmbH
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Buch. Condizione: Neu. Druck auf Anfrage Neuware - Printed after ordering - Structure-based (SBDD) and ligand-based (LBDD) drug design are extremely important and active areas of research in both the academic and commercial realms. This book provides a complete snapshot of the field of computer-aided drug design and associated e…xperimental approaches. The wide range of topics covered here is useful to the practising chemist, medicinal chemist, or structural biologist.
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Da: Kennys Bookshop and Art Galleries Ltd., Galway, GY, IrlandaKennys Bookshop and Art Galleries Ltd.
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Condizione: New. This book provides a complete snapshot of various experimental approaches to structure-based and ligand-based drug design and is illustrated with more than 200 images. Editor(s): Merz, Kenneth M., Jr., PhD; Ringe, Dagmar; Reynolds, Charles H. Num Pages: 286 pages, 204 b/w illus. 26 tables. BIC Classification: MM…G. Category: (P) Professional & Vocational. Dimension: 279 x 215 x 18. Weight in Grams: 1210. . 2010. Illustrated. hardcover. . . . .
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Da: Brook Bookstore On Demand, Napoli, NA, ItaliaBrook Bookstore On Demand
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Condizione: new. Questo è un articolo print on demand.
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Condizione: new. Questo è un articolo print on demand.
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Da: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, GermaniaBuchWeltWeit Ludwig Meier e.K.
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Taschenbuch. Condizione: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -A solution to the protein folding problem has eluded researchers for more than 30 years. The stakes are high. Such a solution will make 40,000 more tertiary structures available for immediate study by translating the DNA sequence i…nformation in the sequence databases into three-dimensional protein structures. This translation will be indispensable for the analy sis of results from the Human Genome Project, de novo protein design, and many other areas of biotechnological research. Finally, an in-depth study of the rules of protein folding should provide vital clues to the protein fold ing process. The search for these rules is therefore an important objective for theoretical molecular biology. Both experimental and theoretical ap proaches have been used in the search for a solution, with many promising results but no general solution. In recent years, there has been an exponen tial increase in the power of computers. This has triggered an incredible outburst of theoretical approaches to solving the protein folding problem ranging from molecular dynamics-based studies of proteins in solution to the actual prediction of protein structures from first principles. This volume attempts to present a concise overview of these advances. Adrian Roitberg and Ron Elber describe the locally enhanced sam pling/simulated annealing conformational search algorithm (Chapter 1), which is potentially useful for the rapid conformational search of larger molecular systems. 596 pp. Englisch.
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Da: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, GermaniaBuchWeltWeit Ludwig Meier e.K.
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EUR 106,99
EUR 23,00 spedizioneSpedito da Germania a U.S.A.Quantità: 2 disponibili
Taschenbuch. Condizione: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -The interface between a living cell and the surrounding world plays a critical role in numerous complex biological processes. Sperm/egg fusion, virus/cell fusion, exocytosis, endocytosis, and ion permeation are a few examples of pr…ocesses involving membranes. In recent years, powerful tools such as X-ray crystal lography, electron microscopy, nuclear magnetic resonance, and infra-red and Raman spectroscopy have been developed to characterize the structure and dy namics of biomembranes. Despite this progress, many of the factors responsible for the function of biomembranes are still not well understood. The membrane is a very complicated supramolecular liquid-crystalline structure that is largely composed of lipids, forming a bilayer, to which proteins and other biomolecules are anchored. Often, the lipid bilayer environment is pictured as a hydropho bic structureless slab providing a thermodynamic driving force to partition the amino acids of a membrane protein according to their solubility. However, much of the molecular complexity of the phospholipid bilayer environment is ignored in such a simplified view. It is likely that the atomic details of the polar head group region and the transition from the bulk water to the hydrophobic core of the membrane are important. An understanding of the factors responsible for the function of biomembranes thus requires a better characterization at the molec ular level of how proteins interact with lipid molecules, of how lipids affect protein structure and of how lipid molecules might regulate protein function. 612 pp. Englisch.
