Membrane Protein Structure and Function Characterization, Jean-Jacques Lacapere
Автор: Jean-Jacques Lacap?re Название: Membrane Protein Structure Determination ISBN: 1493961179 ISBN-13(EAN): 9781493961177 Издательство: Springer Рейтинг: Цена: 20962.00 р. Наличие на складе: Есть у поставщика Поставка под заказ.
Описание: Part I: Membrane Protein Purification 1. Characterization of Membrane Protein Preparations: Measurement of Detergent Content and Ligand Binding after Proteoliposomes Reconstitution Mariano A. Ostuni, Soria Iatmanen, David Teboul, Jean-Claude Robert, and Jean-Jacques Lacapиre 2. Native Membrane Proteins Versus Yeast Recombinant: An Example, the Mitochondrial ADP/ATP Carrier Bertrand Arnou, Cйcile Dahout-Gonzalez, Ludovic Pelosi, Guy J.-M. Lauquin, Gйrard Brandolin, and Vйronique Trйzйguet 3. Bacterial Overexpressed Membrane Proteins: An Example, the TSPO Jean-Claude Robert and Jean-Jacques Lacapиre 4. Insect Cell Versus Bacterial Overexpressed Membrane Proteins: An Example, the Human ABCG2 Transporter Alexandre Pozza, Josй M. Perez-Victoria, and Attilio Di Pietro Part II: X-Ray Crystallography 5. Crystallography of Membrane Proteins: From Crystallization to Structure Aurйlien Deniaud, Ekaterina Moiseeva, Valentin Gordeliy, and Eva Pebay-Peyroula 6. Structural Approaches of the Mitochondrial Carrier Family Hughes Nury, Iulia Blesneac, Stephanie Ravaud, and Eva Pebay-Peyroula 7. What Can Be Learned about the Function of a Single Protein from Its Various X-Ray Structures: The Example of the Sarcoplasmic Calcium Pump Jesper Vuust M ller, Claus Olesen, Anne-Marie Lund Winther, and Poul Nissen 8. Toward Drug Design: Recent Progress in the Structure of GPCR, a Membrane Protein with High Potential as a Pharmaceutical Target Vadim Cherezov, Enrique Abola, and Raymond C. Stevens Part III: Electron Microscopy 9. Observation of Membrane Proteins in situ: AQPcic, the Insect Aquaporin Example Daniel Thomas and Annie Cavalier 10. Two-Dimensional Crystallization of Integral Membrane Proteins for Electron Crystallography David L. Stokes, William J. Rice, Minghui Hu, Changki Kim, and Iban Ubarretxena 11. Structure Determination of Membrane Protein by Both Cryo Electron Tomography and Single Particle Analysis Sylvain Trйpout, Jean-Christophe Taveau, and Olivier Lambert 12. Electron Microscope Tomography of Native Membranes Gabriel Pйranzi, Cedric Messaoudi, Leeyah Issop, and Jean-Jacques Lacapиre 13. From Electron Microscopy Maps to Atomic Structures Using Normal Mode-Based Fitting Konrad Hinsen, Edward Beaumont, Bertrand Fournier, and Jean-Jacques Lacapиre Part IV: Nuclear Magnetic Resonance 14. Determination of Membrane Protein Structures Using Solution and Solid-State NMR Pierre Montaville and Nadиge Jamin 15. Membrane Protein Fragments Reveal Both Secondary and Tertiary Structure of Membrane Proteins Philip L. Yeagle and Arlene D. Albert 16. What Can We Learn From a Small Regulatory Membrane Protein? Gianluigi Veglia, Kim N. Ha, Lei Shi, Raffaello Verardi, and Nathaniel J. Traaseth 17. Solution-State NMR Spectroscopy for Investigating 3D Structure of Membrane Proteins in Detergent Micelles: Structure of the Klebsiella pneumoniae Outer Membrane Protein, KpOmpA Marie Renault, Olivier Saurel, Pascal Demange, Virginie Reat, and Alain Milon 18. NMR Spectroscopy of Lipid Bilayers Axelle Grйlard, Cйcile Loudet, Anna Diller, and Erick J. Dufourc Part V: Molecular Modelling 19. Critical Review of General Guidelines for Membrane Proteins Model Building and Analysis Catherine Etchebest and Gaelle Debret 20. 3D-Structural Models of Transmembrane Proteins Alexandre G. de Brevern 21. Molecular Dynamics of Membrane Peptides and Proteins: Principles and Comparison to Experimental Data Patrick F.J. Fuchs 22. Membrane Protein Dynamics from Femtoseconds to Seconds Christian Kandt and Luca Monticelli 23. The Family of G Protein-Coupled Receptors: An Example of Membrane Proteins Irina G. Tikhonova and Daniel Fourmy
1. Composition and dynamics of the eukaryotic replisome: a brief overview;Stuart A. MacNeill 1.1 Introduction 1.2 Replication origins and the origin recognition complex 1.3 Formation of the pre-RC at origins 1.4 The replisome progression complex 1.5 The replicative polymerases 1.6 Sliding clamp and clamp loader complexes 1.7 Okazaki fragment processing 1.8 Model systems for the studying eukaryotic replication 1.8.1 SV40 1.8.2 Yeast 1.8.3 Xenopus 1.8.4 Archaea 1.8.5 Other model systems 1.9 Conclusions Acknowledgements References
2. Evolutionary diversification of eukaryotic DNA replication machinery; Stephen J. Aves, Yuan Liu and Thomas A. Richards 2.1 Introduction 2.2 Eukaryotic diversity 2.3 Conservation of replisome proteins 2.4 Indispensable replisome proteins 2.5 Replisome proteins present in all eukaryotic supergroups 2.6 Replisome proteins not present in all supergroups 2.7 A complex ancestral replisome 2.8 Conclusions References
3. The origin recognition complex: a biochemical and structural view; Huilin Li and Bruce Stillman 3.1 Introduction 3.2 The S. cerevisiae ORC 3.3 The S. pombe ORC 3.4 The D. melanogaster ORC 3.5 The H. sapiens ORC 3.6 Future perspectives Acknowledgements References
4. Archaeal Orc1/Cdc6 Proteins; Stephen D. Bell 4.1 Introduction 4.2 Origins of DNA replication in the Archaea 4.3 Orc1/Cdc6 Structure 4.4 Structures of Orc1/Cdc6 bound to DNA 4.5 Beyond binding origins - what do Orc1/Cdc6s do?Acknowledgements References
5. Cdt1 and Geminin in DNA replication initiation; Christophe Caillat and Anastassis Perrakis 5.1 Cdt1 and Geminin: a functional preview5.2 The multiple faces of Geminin 5.2.1 Geminin functions in replication licensing 5.2.2 Geminin in the cell cycle 5.2.3 Geminin in cell differentiation 5.3 The structure of Geminin 5.3.1 The N-terminal domain 5.3.2 The coiled-coil domain 5.4 The structure of Cdt1 5.4.1 The N-terminal domain is highly regulated 5.4.2 The structurally conserved winged helix domains 5.4.3 The recruitment of Cdt1 on chromatin 5.5 The Cdt1-Geminin complex 5.5.1 The primary and secondary interfaces 5.5.2 The tertiary interface 5.5.3 Conformational change of the N-terminal domain? 5.6 Models for a Cdt1-Geminin molecular switch 5.7 Conclusions References
6. MCM structure and mechanics: what we have learned from archaeal MCM: Ian M. Slaymaker and Xiaojiang S. Chen 6.1 Introduction 6.2 Complex organization: Hexamers and double hexamers 6.3 Helicase activity 6.3.1 Steric exclusion 6.3.2 Ploughshare 6.3.3 LTag looping model (or strand exclusion) 6.3.4 Rotary pump 6.4 Domains and features of an MCM subunit 6.4.1 N domain 6.4.2 C domain 6.4.2.1 ATP binding pocket 6.4.2.2 Hairpins, helices and inserts 6.4.2.3 Winged helix domain 6.5 Inter- and intra-subunit communication 6.6 Higher-order MCM oligomers 6.7 Conclusions References
7. The Eukaryotic Mcm2-7 Replicative Helicase; Sriram Vijayraghavan and Anthony Schwacha 7.1 Introduction 7.2 The 'Mcm problem' and nonequivalent ATPase active sites 7.3 Discovery of Mcm2-7 helicase activity and the Mcm2/5 gate 7.3.1 Differences in circular ssDNA binding between Mcm2-7 and Mcm467 7.3.2 An in vitro condition that 'closes' Mcm2-7 stimulates its helicase activity 7.3.3 The Mcm2/5 'gate' model - the open conformation and DNA unwinding are mutually exclusive 7.4 The CMG complex 7.4.1 Discovery of the CMG complex 7.4.2 CMG structure - Cdc45 and GINS close the Mcm2/5 gate 7.4.3 Possible regu
Автор: Wolfgang B. Fischer Название: Viral Membrane Proteins: Structure, Function, and Drug Design ISBN: 1441934537 ISBN-13(EAN): 9781441934536 Издательство: Springer Рейтинг: Цена: 27950.00 р. Наличие на складе: Есть у поставщика Поставка под заказ.
Описание: The range of information covered includes signal proteins, ion channels, and fusion proteins.This book has a place in the libraries of researchers and scientists in a wide array of fields, including protein chemistry, molecular biophysics, pharmaceutical science and research, bioanotechnology, molecular biology, and biochemistry.
Автор: Hieronim Jakubowski Название: Homocysteine in Protein Structure/Function and Human Disease ISBN: 3709117208 ISBN-13(EAN): 9783709117200 Издательство: Springer Рейтинг: Цена: 18167.00 р. Наличие на складе: Есть у поставщика Поставка под заказ.
Описание: Excess of homocysteine, a product of the metabolism of the essential amino acid methionine, is associated with poor health, is linked to heart and brain diseases in general human populations, and accelerates mortality in heart disease patients. Neurological and cardiovascular abnormalities occur in patients with severe genetic hyperhomocysteinemia and lead to premature death due to vascular complications. Although it is considered a non-protein amino acid, studies over the past dozen years have discovered mechanisms by which homocysteine becomes a component of proteins. Homocysteine-containing proteins lose their normal biological function and become auto-immunogenic and pro-thrombotic. In this book, the author, a pioneer and a leading contributor to the field, describes up-to date studies of the biological chemistry of homocysteine-containing proteins, as well as pathological consequences and clinical implications of their formation. This is a comprehensive account of the broad range of basic science and medical implications of homocysteine-containing proteins for health and disease.
Автор: Nagarajan Vaidehi; Judith Klein-Seetharaman Название: Membrane Protein Structure and Dynamics ISBN: 1493962337 ISBN-13(EAN): 9781493962334 Издательство: Springer Рейтинг: Цена: 20263.00 р. Наличие на складе: Есть у поставщика Поставка под заказ.
Описание: This Methods in Molecular Biology (TM) book details approaches to the structure, dynamics and interactions of membrane proteins, including measurement procedures and computational methods for structure prediction and insight on the dynamics of membrane receptors.
Описание: This book reviews current techniques used in membrane protein structural biology, with a strong focus on practical issues. The study of membrane protein structures not only provides a basic understanding of life at the molecular level but also helps in the rational and targeted design of new drugs with reduced side effects. Today, about 60% of the commercially available drugs target membrane proteins and it is estimated that nearly 30% of proteins encoded in the human genome are membrane proteins. In recent years much effort has been put towards innovative developments to overcome the numerous obstacles associated with the structure determination of membrane proteins. This book reviews a variety of recent techniques that are essential to any modern researcher in the field of membrane protein structural biology. The topics that are discussed are not commonly found in textbooks. The scope of this book includes: * Expression screening using fluorescent proteins * The use of detergents in membrane protein research * The use of NMR * Synchrotron developments in membrane protein structural biology * Visualisation and X-ray data collection of microcrystals * X-ray diffraction data analysis from multiple crystals * Serial millisecond crystallography * Serial femtosecond crystallography * Membrane protein structures in drug discovery The information provided in this book should be of interest to anyone working in the area of structural biology. Students will find carefully prepared overviews of basic ideas and advanced protein scientists will find the level of detail required to apply the material directly to their day to day work. Chapters 4, 5, 6, 8 and 9 of this book are published open access under a CC BY 4.0 license at link.springer.com.
Автор: D.L. Smith; Z.H. Zaidi Название: Protein Structure — Function Relationship ISBN: 1461380154 ISBN-13(EAN): 9781461380153 Издательство: Springer Рейтинг: Цена: 14673.00 р. Наличие на складе: Есть у поставщика Поставка под заказ.
Описание: Although many pursue understanding of the relationship between protein structure and function for the thrill of pure science, the pay-off in a much broader sense is the ability to manipulate the Earth`s chemistry and biology to improve the quality of life for mankind.
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