Perspectives on Solid State NMR in Biology

ISBN-13: 9780792371021 / Angielski / Twarda / 2001 / 233 str.

S. R. Kiihne; H. J. M. de Groot; S. R. Kiihne

Opis

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.

Spis treści

Preface. List of Conference Organizers. List of Conference Speakers. Section I: Advances in MAS Techniques for Non-Aligned Systems. Using Symmetry to Design Pulse Sequences in Solid-State NMR; A. Brinkmann, et al. Accurate 13C-15N Distance Measurements in Uniformly 13C,15N-Labeled Peptides; C.P. Jaroniec, et al. Selectivity of Double-Quantum Filtered Rotational-Resonance Experiments on Larger-than-Two-Spin Systems; M. Bechmann, et al. Multiple-Quantum Spectroscopy of Fully Labeled Polypeptides Under MAS: A Statistical and Experimental Analysis; S. Luca, et al. Section II: Advances in Techniques for Aligned Systems. 2H, 15N and 31P Solid-State NMR Spectroscopy of Polypeptides Reconstituted Into Oriented Phospholipid Membranes; B. Bechinger, et al. From Topology to High Resolution Membrane Protein Structures; T.A. Cross, et al. Toward Dipolar Recoupling in Macroscopically Ordered Samples of Membrane Proteins Rotating at the Magic Angle; C. Glaubitz, et al. Solid State 19F-NMR of Biomembranes; S.L. Grage, et al. Section III: Important Technologies. Numerical Simulations for Experiment Design and Extraction of Structural Parameters in Biological Solid-State NMR Spectroscopy; M. Bak, et al. An Ab-Initio Molecular Dynamics Modeling of the Primary Photochemical Event in Vision; F. Buda, et al. Refolded G protein-coupled Receptors from E. coli Inclusion Bodies; H. Kiefer, et al. Semliki Forest Virus Vectors: Versatile Tools for Efficient Large-Scale Expression of Membrane Receptors; K. Lundstrom. G Protein-Coupled Receptor Expression in Halobacterium salinarum; A.M. Winter-Vann, et al. Magnetic Resonance Microscopy for Studying the Development of Chicken and Mouse Embryos; R.E. Poelmann, et al. Section IV: Applications in Membrane Proteins and Peptides. MAS NMR on a Uniformly [13C,15N] Labeled LH2 Light-Harvesting Complex from Rhodopseudomonas Acidophila 10050 at Ultra-High Magnetic Fields; T.A. Egorova-Zachernyuk, et al. Determination of Torsion Angles in Membrane Proteins; J.C. Lansing, et al. Characterization and Assignment of Uniformly Labeled NT(8-13) at the Agonist Binding Site of the G-Protein Coupled Neurotensin Receptor; P.T.F. Williamson, et al. Structural Insight into the Interaction of Amylod-&bgr; Peptide with Biological Membranes by Solid State NMR; G. Gröbner, et al. Photochemically Induced Dynamic Nuclear Polarization in Bacterial Photosynthetic Reaction Centres Observed by 13C Solid-State NMR; J. Matysik, et al. Index.