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Solid state NMR is rapidly emerging as a universally applicable method for the characterization of ordered structures that cannot be studied with solution methods or diffraction techniques. This proceedings -; from a recent international workshop - captures an image of the latest developments and future directions for solid state NMR in biological research, particularly on membrane proteins. Detailed information on how hormones or drugs bind to their membrane receptor targets is needed, e.g. for rational drug design. Higher fields are bringing clear improvements, and the power of solid state NMR techniques for studying amorphous and membrane associated peptides, proteins and complexes is shown by examples of applications at ultra-high fields. Progress in protein expression, experimental design and data analysis are also presented by leaders in these research areas.




Solid state NMR is rapidly emerging as a universally applicable method for the characterization of ordered structures that cannot be studied with solution methods or diffraction techniques. This proceedings -; from a recent international workshop - captures an image of the latest developments and future directions for solid state NMR in biological research, particularly on membrane proteins. Detailed information on how hormones or drugs bind to their membrane receptor targets is needed, e.g. for rational drug design. Higher fields are bringing clear improvements, and the power of solid state NMR techniques for studying amorphous and membrane associated peptides, proteins and complexes is shown by examples of applications at ultra-high fields. Progress in protein expression, experimental design and data analysis are also presented by leaders in these research areas.


Solid state NMR is rapidly emerging as a universally applicable method for the characterization of ordered structures that cannot be studied with solution methods or diffraction techniques. This proceedings -; from a recent international workshop - captures an image of the latest developments and future directions for solid state NMR in biological research, particularly on membrane proteins. Detailed information on how hormones or drugs bind to their membrane receptor targets is needed, e.g. for rational drug design. Higher fields are bringing clear improvements, and the power of solid state NMR techniques for studying amorphous and membrane associated peptides, proteins and complexes is shown by examples of applications at ultra-high fields. Progress in protein expression, experimental design and data analysis are also presented by leaders in these research areas.
Content:
Front Matter....Pages i-xi
Front Matter....Pages 1-1
Using symmetry to design pulse sequences in solid-state NMR....Pages 3-14
Accurate 13C-15N Distance Measurements in Uniformly 13C,15N-Labeled Peptides....Pages 15-21
Selectivity of Double-Quantum Filtered Rotational-Resonance Experiments on Larger-than-Two-Spin Systems....Pages 23-31
Multiple-quantum spectroscopy of fully labeled polypeptides under MAS: A statistical and experimental analysis....Pages 33-41
Front Matter....Pages 43-43
2H, 15N and 31P solid-state NMR spectroscopy of polypeptides reconstituted into oriented phospholipid membranes....Pages 45-53
From Topology to High Resolution Membrane Protein Structures....Pages 55-69
Toward dipolar recoupling in macroscopically ordered samples of membrane proteins rotating at the magic angle....Pages 71-81
Solid state 19F-NMR of biomembranes....Pages 83-91
Front Matter....Pages 93-93
Numerical simulations for experiment design and extraction of structural parameters in biological solid-state NMR spectroscopy....Pages 95-109
An ab-initio molecular dynamics modeling of the primary photochemical event in vision....Pages 111-122
Refolded G protein-coupled receptors from E. coli inclusion bodies....Pages 123-130
Semliki Forest virus vectors: versatile tools for efficient large-scale expression of membrane receptors....Pages 131-139
G protein-coupled receptor expression in Halobacterium salinarum ....Pages 141-159
Magnetic resonance microscopy for studying the development of chicken and mouse embryos....Pages 161-167
Front Matter....Pages 169-169
MAS NMR on a uniformly [13C, 15N] labeled LH2 light-harvesting complex from Rhodopseudomonas acidophila 10050 at ultra-high magnetic fields....Pages 171-183
Determination of Torsion Angles in Membrane Proteins....Pages 185-190
Characterization and assignment of uniformly labeled NT(8–13) at the agonist binding site of the G-protein coupled neurotensin receptor....Pages 191-201
Structural insight into the interaction of amyloid-? peptide with biological membranes by solid state NMR....Pages 203-214
Photochemically induced dynamic nuclear polarization in bacterial photosynthetic reaction centres observed by 13C solid-state NMR....Pages 215-225
Back Matter....Pages 227-233


Solid state NMR is rapidly emerging as a universally applicable method for the characterization of ordered structures that cannot be studied with solution methods or diffraction techniques. This proceedings -; from a recent international workshop - captures an image of the latest developments and future directions for solid state NMR in biological research, particularly on membrane proteins. Detailed information on how hormones or drugs bind to their membrane receptor targets is needed, e.g. for rational drug design. Higher fields are bringing clear improvements, and the power of solid state NMR techniques for studying amorphous and membrane associated peptides, proteins and complexes is shown by examples of applications at ultra-high fields. Progress in protein expression, experimental design and data analysis are also presented by leaders in these research areas.
Content:
Front Matter....Pages i-xi
Front Matter....Pages 1-1
Using symmetry to design pulse sequences in solid-state NMR....Pages 3-14
Accurate 13C-15N Distance Measurements in Uniformly 13C,15N-Labeled Peptides....Pages 15-21
Selectivity of Double-Quantum Filtered Rotational-Resonance Experiments on Larger-than-Two-Spin Systems....Pages 23-31
Multiple-quantum spectroscopy of fully labeled polypeptides under MAS: A statistical and experimental analysis....Pages 33-41
Front Matter....Pages 43-43
2H, 15N and 31P solid-state NMR spectroscopy of polypeptides reconstituted into oriented phospholipid membranes....Pages 45-53
From Topology to High Resolution Membrane Protein Structures....Pages 55-69
Toward dipolar recoupling in macroscopically ordered samples of membrane proteins rotating at the magic angle....Pages 71-81
Solid state 19F-NMR of biomembranes....Pages 83-91
Front Matter....Pages 93-93
Numerical simulations for experiment design and extraction of structural parameters in biological solid-state NMR spectroscopy....Pages 95-109
An ab-initio molecular dynamics modeling of the primary photochemical event in vision....Pages 111-122
Refolded G protein-coupled receptors from E. coli inclusion bodies....Pages 123-130
Semliki Forest virus vectors: versatile tools for efficient large-scale expression of membrane receptors....Pages 131-139
G protein-coupled receptor expression in Halobacterium salinarum ....Pages 141-159
Magnetic resonance microscopy for studying the development of chicken and mouse embryos....Pages 161-167
Front Matter....Pages 169-169
MAS NMR on a uniformly [13C, 15N] labeled LH2 light-harvesting complex from Rhodopseudomonas acidophila 10050 at ultra-high magnetic fields....Pages 171-183
Determination of Torsion Angles in Membrane Proteins....Pages 185-190
Characterization and assignment of uniformly labeled NT(8–13) at the agonist binding site of the G-protein coupled neurotensin receptor....Pages 191-201
Structural insight into the interaction of amyloid-? peptide with biological membranes by solid state NMR....Pages 203-214
Photochemically induced dynamic nuclear polarization in bacterial photosynthetic reaction centres observed by 13C solid-state NMR....Pages 215-225
Back Matter....Pages 227-233
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