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Umfang: 1 Online-Ressource (getrennte Seitenzählung) , Illustrationen, Diagramme

Ausgabe: Version: 20201201

ISBN: 9780750325325 , 9780750325318

Serie: Biophysical Society-IOP series

Inhalt: The purpose of this book is to describe the methodology and applications of solid-state NMR spectroscopy to studies of membrane proteins, membrane-active peptides and model biological membranes. As well as structural studies, this book contains coverage of membrane interactions and molecular motions. Advances in biological solid-state NMR are very pertinent with high-field developments seeing applications in biological membranes and whole cells. Experts who are leaders in the development and application of biological solid-state NMR are chapter contributors. Part of Biophysical Society-IOP series.

Weitere Ausg.: ISBN 9780750325301

Weitere Ausg.: ISBN 9780750325332

Weitere Ausg.: Erscheint auch als Druckausgabe Solid-state NMR Bristol, UK : IOP Publishing, 2020 ISBN 075032533X

Weitere Ausg.: ISBN 9780750325301

Weitere Ausg.: ISBN 9780750325332

Sprache: Englisch

DOI: 10.1088/978-0-7503-2532-5

URL: Volltext  (lizenzpflichtig)

URL: Volltext  (lizenzpflichtig)

UID:

Umfang: 1 online resource (416 pages)

Ausgabe: 1st ed.

ISBN: 9780750341073

Serie: Biophysical Society-IOP Series

Inhalt: This book describes the methodology and applications of solid-state NMR spectroscopy to studies of membrane proteins, membrane-active peptides and model biological membranes. As well as structural studies, this book contains coverage of membrane interactions and molecular motions. All chapter contributors are experts and leaders in the development and application of biological solid-state NMR.

Anmerkung: Intro -- Preface -- Foreword -- Outline placeholder -- Biomembranes: the Holy Grail -- Editor biographies -- Frances Separovic -- Marc-Antoine Sani -- List of contributors -- Chapter 1 Solid-state NMR methods for studying membrane systems -- Overview -- 1.1 Introduction -- 1.2 Using NMR as a reporter on membrane structure -- 1.3 Dynamics in biological membranes -- 1.4 Probing the surface charge of membranes with solid-state NMR -- 1.5 Lateral domain formation -- 1.6 Lipid/protein interactions -- 1.6.1 Insight into protein/lipid headgroup association by 31P CP MAS NMR -- 1.6.2 Studying annular lipids bound to integral membrane proteins -- 1.6.3 Studying non-annular lipids bound to integral membrane proteins -- 1.7 Membrane remodeling -- 1.8 Summary -- Acknowledgements -- References -- Chapter 2 Characterization of lipid behaviour in model biomembranes using 2H solid-state NMR -- Abstract -- 2.1 Introduction -- 2.2 The quadrupole interaction -- 2.3 The wideline 2H NMR spectra of chain-deuterated phospholipids in bilayers -- 2.4 The quadrupole echo -- 2.5 Characterizing phospholipid bilayer phases using wideline 2H NMR -- 2.6 Using spectral subtraction to identify boundaries of two-phase coexistence regions in bilayer temperature-composition phase diagrams -- 2.7 Beyond difference spectroscopy-defining liquid crystalline phase coexistence with 2H NMR -- 2.8 Summary -- References -- Chapter 3 Deuterium solid-state NMR of whole bacteria: sample preparation and effects of cell envelope manipulation -- Overview -- 3.1 Structure and composition of bacterial cell envelopes -- 3.2 Sample preparation -- 3.3 Static 2H NMR of Gram(−) and Gram(+) bacteria -- 3.4 2H NMR of bacteria with cell envelope perturbation -- 3.5 What have we learned from 2H NMR of bacteria so far? -- References -- Chapter 4 Solid-state NMR study of microalgal membranes and cell walls. , Abstract -- 4.1 Overview -- 4.2 Microalgal cell membrane composition and architecture -- 4.2.1 Microalgal cell wall and plasma membrane -- 4.2.2 Photosynthetic organelles (thylakoids and chloroplast) -- 4.2.3 lipid droplets and free fatty acids -- 4.3 Technical considerations -- 4.3.1 Observable nuclei for microalgal membranes studies -- 4.3.2 Solution and solid-state NMR -- 4.4 NMR of lipid extracts and model membranes -- 4.5 In vivo, in-cell and in situ NMR -- 4.5.1 1H-NMR based approaches -- 4.5.2 1D 13C solid-state NMR methods -- 4.5.3 2D-13C and 15N-NMR experiments -- 4.6 Conclusion and future prospects -- Acknowledgements -- References -- Chapter 5 Determining the mechanism of action of host defense peptides: solid-state NMR approaches -- Abstract -- 5.1 Introduction -- 5.2 Model membranes -- 5.3 Whole cells -- 5.4 Conclusions -- References -- Chapter 6 19F NMR of biomembranes -- Abstract -- 6.1 Introduction -- 6.2 19F NMR -- 6.2.1 Advantages of 19F as NMR probe -- 6.2.2 Limitations of 19F NMR -- 6.2.3 19F NMR bridges the gap -- 6.2.4 Hardware requirements -- 6.2.5 Typical 19F NMR chemical shifts -- 6.3 Introducing 19F into biomembranes -- 6.3.1 19F-labels -- 6.3.2 Biosynthetic incorporation of 19F -- 6.3.3 Chemical introduction of 19F -- 6.4 Line narrowing techniques for 19F NMR of biomembranes -- 6.4.1 Multipulse solid-state 19F NMR -- 6.4.2 Oriented samples for solid-state 19F NMR -- 6.4.3 Magic angle spinning 19F NMR -- 6.4.4 Solution NMR of membrane proteins in membrane mimetics -- 6.5 Solid-state 19F NMR distance measurements in biomembranes -- 6.5.1 Distance measurements in oriented samples -- 6.5.2 Distance measurements under MAS -- 6.5.3 Multidimensional solid-state 19F NMR experiments -- 6.5.4 Ligands bound to membrane proteins -- 6.5.5 Intermolecular interactions of oligomeric membrane proteins and peptides. , 6.5.6 Distance measurements in solution -- 6.6 Solid-state 19F NMR orientation measurements in biomembranes -- 6.6.1 Orientation dependence in solid-state 19F NMR -- 6.6.2 Mobility and orientation -- 6.6.3 Molecular orientation in membranes from 19F NMR on oriented samples -- 6.6.4 Peptide re-alignment transitions in membranes revealed by solid-state 19F NMR -- 6.6.5 Peptide mobility in membranes -- 6.6.6 Orientation and mobility of lipids and small lipid-soluble molecules -- 6.7 Probing the environment -- 6.7.1 Conformational changes -- 6.7.2 Probing solvent environment -- 6.8 19F NMR in native membranes -- 6.9 Conclusions -- Acknowledgements -- References -- Chapter 7 Structure, topology and dynamics of membrane-associated peptides by solid-state NMR -- Summary -- 7.1 Introduction -- 7.2 Solid-state NMR spectroscopic approaches -- 7.3 The anisotropy of solid-state NMR interactions -- 7.4 Sample preparation -- 7.4.1 Peptides -- 7.4.2 Sample preparation: bicelles and supported lipid bilayer -- 7.5 Oriented solid-state NMR spectroscopy to study the conformation, topology and dynamics of peptides in membranes -- 7.6 Sample heterogeneity and orientational distributions -- 7.7 Membrane lipid composition -- 7.8 Taking peptide motions into consideration -- 7.9 Signal enhancement by DNP -- Acknowledgement -- References -- Chapter 8 Solid-state NMR and dynamic nuclear polarization studies of molecular interactions in membranes -- Abstract -- 8.1 Introduction -- 8.2 Membranes in the presence of small organic molecules -- 8.3 Membrane-active proteins and peptides -- 8.4 Transmembrane proteins -- 8.5 Membrane studies by NMR -- 8.6 Native membranes -- 8.7 Wideline and oriented membranes NMR -- 8.7.1 Deuterium NMR -- 8.7.2 Lipid phase analysis by 31P wideline NMR -- 8.7.3 High resolution NMR in oriented membranes - 15N PISEMA. , 8.8 High resolution sample spinning solid-state NMR -- 8.8.1 Membrane studies by 13C MAS NMR -- 8.8.2 Membrane interactions monitored by 31P MAS NMR -- 8.8.3 Correlation NMR spectroscopy in membranes -- 8.9 Dynamic nuclear polarization -- 8.10 Summary -- Acknowledgements -- References -- Chapter 9 Mapping dynamics in membrane proteins with solid-state NMR: methods and examples -- 9.1 Introduction -- 9.2 NMR strategies to monitor dynamics -- 9.3 Monitoring dynamics with CP-based methods -- 9.3.1 WISE -- 9.3.2 CPPI -- 9.3.3 LG-CP -- 9.3.4 Dynamics in oriented NMR -- 9.4 Monitoring dynamics with heteronuclear DD recoupling-based methods -- 9.4.1 DIPSHIFT -- 9.4.2 REDOR -- 9.4.3 Symmetry-based schemes -- 9.5 Monitoring dynamics with CSA recoupling methods -- 9.5.1 2DCSA and SUPER -- 9.5.2 Symmetry-based schemes for CSA recoupling -- 9.6 Examples of studying dynamics in membrane proteins -- 9.6.1 Cross-polarisation based filtering -- 9.6.2 Rotational-echo based experiments -- 9.6.3 Protein structures using SLF experiments -- 9.7 Schemes for higher MAS and stronger couplings -- 9.7.1 REDOR-schemes with dipole-dipole coupling scaling -- 9.7.2 Equivalence of DIPSHIIT and REDOR pulse schemes -- 9.7.3 DIPSHIFT and REDOR at higher MAS frequencies -- 9.8 Conclusions -- Acknowledgements -- References -- Chapter 10 Solid-state NMR studies of peripherally membrane-associated proteins: dealing with dynamics, disorder and dilute conditions -- Abstract -- 10.1 Peripheral and conditional membrane proteins -- 10.1.1 What are peripheral membrane proteins? -- 10.1.2 Structural studies of peripheral membrane proteins. -- 10.2 Solid-state NMR studies of peripheral membrane proteins -- 10.3 Case studies of ssNMR on peripheral membrane proteins -- 10.3.1 Lipid-bound cytochrome c as a pro-apoptotic lipid peroxidase -- 10.3.2 Myelin basic protein. , 10.3.3 The Pleckstrin homology domain of PLC-δ1 -- 10.4 Lessons learned -- 10.5 Conclusions -- Acknowledgements -- References -- Chapter 11 Structural dynamics of G protein-coupled receptors in lipid membranes investigated by solid-state NMR spectroscopy -- Overview/Abstract -- 11.1 Introduction -- 11.2 Preparative options for studying GPCRs by NMR spectroscopic tools -- 11.2.1 Construct optimization and expression systems -- 11.2.2 Isotopic labeling -- 11.2.3 Reconstitution into membranes and membrane mimetics -- 11.3 Methodological options for studying dynamics of GPCRs by solid-state NMR -- 11.3.1 Isotropic chemical shift changes -- 11.3.2 Influence of motions on anisotropic chemical shift interactions -- 11.3.3 Molecular order parameters -- 11.3.4 Relaxation rates -- 11.4 Examples -- 11.4.1 Chemokine receptor CXCR1 -- 11.4.2 Neuropeptide Y receptor type 2 -- 11.4.3 Growth hormone secretagogue receptor -- 11.5 Conclusions -- Acknowledgement -- References -- Chapter 12 Hybridizing isotropic and anisotropic solid-state NMR restraints for membrane protein structure determination -- Abstract -- 12.1 Oriented-sample solid-state NMR (OS-ssNMR) structure determination of membrane proteins -- 12.2 Chemical shift anisotropy -- 12.3 Dipolar coupling -- 12.4 Scaling of orientational restraints due to conformational and topological dynamics -- 12.5 Hybridization of isotropic and anisotropic restraints -- 12.6 Summary -- Acknowledgments -- References -- Chapter 13 Beyond structure: understanding dynamics in membrane protein complexes -- Overview -- 13.1 Introduction -- 13.2 Membrane protein dynamics -- 13.3 NMR studies of dynamics of specific membrane protein systems -- 13.3.1 Anabaena sensory rhodopsin -- 13.3.2 Outer membrane proteins -- 13.3.3 Bacterial transmembrane chemoreceptors -- 13.4 Conclusions -- Acknowledgement -- References. , Chapter 14 Solid-state NMR methods for investigations of membrane protein structure and dynamics.

Weitere Ausg.: Print version: Separovic, Frances Solid-State NMR Bristol : Institute of Physics Publishing,c2020 ISBN 9780750325332

Sprache: Englisch

Schlagwort(e): Electronic books.

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UID:

Umfang: 1 online resource (various pagings) : , illustrations (some color).

ISBN: 9780750325325 , 9780750325318

Serie: Biophysical Society-IOP series

Inhalt: The purpose of this book is to describe the methodology and applications of solid-state NMR spectroscopy to studies of membrane proteins, membrane-active peptides and model biological membranes. As well as structural studies, this book contains coverage of membrane interactions and molecular motions. Advances in biological solid-state NMR are very pertinent with high-field developments seeing applications in biological membranes and whole cells. Experts who are leaders in the development and application of biological solid-state NMR are chapter contributors. Part of Biophysical Society-IOP series.

Anmerkung: "Version: 20201201"--Title page verso. , 1. Solid-state NMR methods for studying membrane systems / Gerhard Gröbner and Philip Williamson -- 2. Characterization of lipid behaviour in model biomembranes using 2H solid-state NMR / Michael R. Morrow and Jenifer L. Thewalt -- 3. Deuterium solid-state NMR of whole bacteria : sample preparation and effects of cell envelope manipulation / Valerie Booth -- 4. Solid-state NMR study of microalgal membranes and cell walls / Alexandre Poulhazan, Alexandre A. Arnold, Dror E. Warschawski and Isabelle Marcotte -- 5. Determining the mechanism of action of host defense peptides : solid-state NMR approaches / Suzana K. Straus, Allen Takayesu and Prashant Kumar -- 6. 19F NMR of biomembranes / Stephan L. Grage, Sergii Afonin and Anne S. Ulrich -- 7. Structure, topology and dynamics of membrane-associated peptides by solid-state NMR / Burkhard Bechinger and Evgeniy Salnikov -- 8. Solid-state NMR and dynamic nuclear polarization studies of molecular interactions in membranes / Vivien Yeh and Boyan B. Bonev -- 9. Mapping dynamics in membrane proteins with solid-state NMR : methods and examples / Kaustubh R. Mote and P.K. Madhu -- 10. Solid-state NMR studies of peripherally membrane-associated proteins : dealing with dynamics, disorder and dilute conditions / Patrick C.A. van der Wel -- 11. Structural dynamics of G protein-coupled receptors in lipid membranes investigated by solid-state NMR spectroscopy / Daniel Huster -- 12. Hybridizing isotropic and anisotropic solid-state NMR restraints for membrane protein structure determination / Daniel K. Weber, Erik K. Larsen, Tata Gopinath and Gianluigi Veglia -- 13. Beyond structure : understanding dynamics in membrane protein complexes / Nikita Malik and Lynmarie Thompson -- 14. Solid-state NMR methods for investigations of membrane protein structure and dynamics / Peng Xiao and Vladimir Ladizhansky -- 15. Proton-detected solid-state NMR and its applications to membrane proteins / Julia Kotschy and Rasmus Linser. , Also available in print. , Mode of access: World Wide Web. , System requirements: Adobe Acrobat Reader, EPUB reader, or Kindle reader.

Weitere Ausg.: Print version: ISBN 9780750325301

Weitere Ausg.: ISBN 9780750325332

Sprache: Englisch

DOI: 10.1088/978-0-7503-2532-5

URL: https://iopscience.iop.org/book/978-0-7503-2532-5