| 书目名称 | Perspectives on Solid State NMR in Biology | | 编辑 | Suzanne R. Kiihne,Huub J. M. Groot | | 视频video | http://file.papertrans.cn/745/744925/744925.mp4 | | 丛书名称 | Focus on Structural Biology | | 图书封面 |  | | 描述 | Solid state NMR is rapidly emerging as a universally applicablemethod for the characterization of ordered structures that cannot bestudied with solution methods or diffraction techniques. Thisproceedings -; from a recent international workshop -captures an image of the latest developments and future directions forsolid state NMR in biological research, particularly on membraneproteins. Detailed information on how hormones or drugs bind to theirmembrane receptor targets is needed, e.g. for rational drug design.Higher fields are bringing clear improvements, and the power of solidstate NMR techniques for studying amorphous and membrane associatedpeptides, proteins and complexes is shown by examples of applicationsat ultra-high fields. Progress in protein expression, experimentaldesign and data analysis are also presented by leaders in theseresearch areas. | | 出版日期 | Book 2001 | | 关键词 | NMR; Resol; biology; proteins; spectroscopy; Biological Microscopy | | 版次 | 1 | | doi | https://doi.org/10.1007/978-94-017-2579-8 | | isbn_softcover | 978-90-481-5744-0 | | isbn_ebook | 978-94-017-2579-8Series ISSN 1571-4853 Series E-ISSN 2542-9566 | | issn_series | 1571-4853 | | copyright | Springer Science+Business Media Dordrecht 2001 |
| 1 |
Using symmetry to design pulse sequences in solid-state NMR |
Andreas Brinkmann,Marina Carravetta,Xin Zhao,Mattias Edén,Jörn Schmedt auf der Günne,Malcolm H. Levitt |
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Abstract
Modern solid-state NMR employs a range of rf pulse sequences for a variety of tasks. There are . sequences which reinforce the averaging effect of the magic-angle rotation, causing different spin species to evolve approximately independently of each other. There are also . sequences which undo the averaging effect of the magic-angle rotation, temporarily restoring couplings which are otherwise inactivated by the sample spinning. The success of solid-state NMR in biological research may depend on the development of decoupling and recoupling pulse sequences which are robust with respect to a variety of undesirable spin interactions and experimental imperfections, and which function over a wide range of static magnetic fields and/or spinning frequencies.
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| 2 |
Accurate 13C-15N Distance Measurements in Uniformly 13C,15N-Labeled Peptides |
C. P. Jaroniec,B. A. Tounge,J. Herzfeld,R. G. Griffin |
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Abstract
The ability to accurately measure .C-.N dipolar couplings corresponding to internuclear distances in the 3–6 Å regime is important for constraining the three-dimensional structure of biological solids. Solid-state NMR (SSNMR) methods for heteronuclear distance measurements in isolated spin pairs are now well-established and will continue to provide valuable structural information [1,2]. However, these methods require synthesis of molecules isotopically labeled in a pairwise fashion, which can be both laborious and expensive. Thus, there is a clear motivation for the development of analogous SSNMR methods for larger spin systems, where multiple internuclear distances can be determined [3–5]. However, in multispin systems .C-.N distance measurements have the potential to be complicated by the presence of multiple homonuclear and heteronuclear spin-spin couplings.
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| 3 |
Selectivity of Double-Quantum Filtered Rotational-Resonance Experiments on Larger-than-Two-Spin Systems |
Matthias Bechmann,Xavier Helluy,Angelika Sebald |
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Abstract
Characterizing the orientation and molecular conformation of small organic molecules bound to the inner or outer surfaces of proteins represents an important step in drug design and in understanding the mechanisms of biochemical reactions, and similarly, of non-biological catalytic reactions. In a biochemical context, such molecular units or subunits may often contain only three or four carbon atoms, examples being the pyruvate anion, fumaric and maleic acid derivatives, or the phosphenolpyruvate moiety in differing degrees of ionization. Magic-angle spinning (MAS) NMR experiments, capable of delivering reliable information about the conformational properties of these molecular units, have to combine several properties in order to be able to fulfill these tasks in realistic application situations. First, the .C resonances originating from the (fully or partially) .C enriched substrate molecules of interest have to be separable from additional natural-abundance .C resonances; this calls for the application of double-quantum filtration (DQF) techniques. Second, many of these small substrate molecules feature structural subunits that require using the orientation dependence of .C chemical shielding as the source of information about molecular conformation; this calls for MAS NMR experiments where magnitudes and orientations of chemical shielding tensors are sensitively reflected. Third, for reasons of synthetic feasibility, the chosen MAS NMR techniques must be applicable in a quantifiable manner to larger-than-two-spin systems. The ease and robustness of the experimental and numerical implementations are an additional consideration.
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| 4 |
Multiple-quantum spectroscopy of fully labeled polypeptides under MAS: A statistical and experimental analysis |
Sorin Luca,Dmitri V. Filippov,Brigitta Angerstein,Gijs A. van der Marel,Jacques H. van Boom,Marc Baldus |
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Abstract
Spectral resolution represents a prerequisite for NMR based structural studies in multior fully labeled polypeptides such as membrane proteins, peptide ligands or protein aggregates. Recent applications in immobilized proteins [1–4] and a membrane protein aggregate [5] revealed that characteristic chemical shift information obtained in the liquid-state improves and expedites spectral assignment under MAS [6] conditions. In many cases, the observed NMR line width may limit applications in polypeptides and proteins of larger size. In this context, correlation experiments are desirable that maximize the spectral resolution without compromising the structural information contained in the spectra.
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| 5 |
2H, 15N and 31P solid-state NMR spectroscopy of polypeptides reconstituted into oriented phospholipid membranes |
Burkhard Bechinger,Christopher Aisenbrey,Christina Sizun,Ulrike Harzer |
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Abstract
Although membrane proteins are abundant and fulfill many important functions, only a few high-resolution conformations of this class of proteins have been published (reviewed in [.]). Structural investigations are hampered by the problems that are encountered during their large-scale expression and purification as well as during application of diffraction and NMR techniques. Since publication of the high-resolution diffraction map of the photoreaction centre [.], the conformations of other bacterial membrane proteins have been solved at a relatively slow pace. Most of these proteins already occur at high concentrations in nature and some of them even in ordered arrays [.]. More recently high resolution structures of eukaryotic membrane proteins have been added to the structural data base, including rhodopsin, a G protein-coupled receptor [.]. Improvements in crystallisation as well as in X-ray and electron diffraction techniques hold promise that these developments will accelerate, and structures of an increasing number of membrane proteins will become available in the future. Some of this work illuminates structural changes that occur during functional activities in a stroboscopic manner [.].
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| 6 |
From Topology to High Resolution Membrane Protein Structures |
T. A. Cross,S. Kim,J. Wang,J. R. Quine |
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Abstract
Structural genomics of membrane proteins represents a particularly exciting challenge for biophysicists. These proteins are heterogeneous, both in themselves because of post translational modifications and in their environment from the heterogeneity of the membrane. Such heterogeneity greatly complicates structural characterization. Furthermore, the scarcity of specific interactions between secondary structural elements in the membrane environment results in increased dynamics and flexibility. Solid state NMR provides a methodology and a range of techniques that can characterize these proteins in a planar lipid bilayer environment [1]. NMR is an inherently high resolution method in that specific atomic sites are directly observed. With solid state NMR this potential for high resolution is fulfilled by obtaining very precise distance and orientational restraints. Until recently however, topology was very difficult to achieve; now several approaches are evolving so that both low resolution topology and unique high resolution structures can be obtained.
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| 7 |
Toward dipolar recoupling in macroscopically ordered samples of membrane proteins rotating at the magic angle |
Clemens Glaubitz,Marina Carravetta,Maffias Edén,Malcolm H. Levitt |
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Abstract
MAS NMR spectroscopy can be combined with the advantages of uniaxially ordered samples of membrane proteins as demonstrated in the so-called MAOSS (magic angle oriented sample spinning) experiment. Under these conditions, dipolar recoupling methods can be used to determine the orientation of internuclear vectors with respect to the MAS rotor frame. However, most approaches to measure dipolar couplings yield angle ambiguities even in the static, non-spinning case. Here, we present the possibility of overcoming these problems by deriving a new homonuclear double-quantum radio frequency pulse sequence based on an eightfold symmetry. Only dipolar Hamiltonian terms with spatial components m=±2 are recoupled with high efficiency allowing unambiguous angle determinations. Preliminary data demonstrate the applicability of this experiment to oriented samples.
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| 8 |
Solid state 19F-NMR of biomembranes |
Stephan L. Grage,Jesús Salgado,Ulrich Dürr,Sergii Afonin,Ralf W. Glaser,Anne S. Ulrich |
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Abstract
Structure determination of membrane-associated polypeptides presents one of the major challenges to solid state NMR spectroscopy. Many studies have been carried out so far using selective isotope labels, such as .H, .C, or .N[1]. These NMR-reporters can be incorporated into the protein backbone or side chains, to reveal local structural parameters and to describe the dynamic properties of the membrane-embedded molecule. For example, an distance . can be measured between a pair of labels by means of dipolar recoupling MAS techniques such as rotational resonance or REDOR[2]. Alternatively, uniaxially oriented samples are used to determine the angle A of a labelled molecular segment with respect to the membrane normal N[3,4,5]. The latter approach relies on the orientation-dependent resonance frequency, which carries information about the anisotropie chemical shift tensor (.C, .N), the dipolar coupling (.H-.N), or the quadrupolar interaction (.H)[6,7].
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| 9 |
Numerical simulations for experiment design and extraction of structural parameters in biological solid-state NMR spectroscopy |
Mads Bak,Robert Schultz,Niels Chr. Nielsen |
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Abstract
Based on a tremendous technological progress, during the past decade it has been demonstrated that solid-state NMR is capable of providing very detailed information about the structure and dynamics of biological molecules in the solid phase. Using state-of-the-art methodology, it is now realistic to resolve, assign, and structurally interpret resonances from peptides/proteins with about 50 – 100 residues and to obtain local structure information for proteins an order of magnitude larger. With considerable room for future development (higher magnetic fields, stronger rf fields, higher spinning speeds, new isotope labeling and expression methods, and new multi-dimensional pulse sequences), these achievements open up exiting perspectives for the study of, e.g., membrane proteins, protein aggregates, and colloids. This is of great importance considering that, e.g., membrane proteins in one way or another are involved in most biological processes . simultaneously may be extremely difficult to characterize at atomic resolution using traditional structure determination methods.
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| 10 |
An ab-initio molecular dynamics modeling of the primary photochemical event in vision |
Francesco Buda,Sylvia I. E. Touw,Huub J. M. de Groot |
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Abstract
In the process of vision, light stimuli are converted into neural information by a membrane protein called rhodopsin that initiates the transduction process. The primary photochemical event involves the photoconversion of rhodopsin into a metastable intermediate called bathorhodopsin [1,2]. The chromophore of rhodopsin is an . retinylidene prosthetic group covalently bound to the surrounding opsin protein via a protonated Schiff base (PSB) linkage to a specific lysine residue, Lys. (Fig. 1). The absorption of light induces the isomerization of the 11-cis-retinal chromophore to an all-. configuration in bathorhodopsin.
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| 11 |
Refolded G protein-coupled receptors from , inclusion bodies |
Hans Kiefer,Klaus Maier,Reiner Vogel |
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Abstract
G protein-coupled receptors (GPCRs) are the largest receptor family in eukaryotes with about 2000 representatives in the human genome. Of these, about 1500 GPCRs transmit signals in intracellular communication, while the remaining part are involved in the recognition of sensory signals such as odorants, gustatory substances and, through the visual pigment rhodopsin, light [1, 2].
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| 12 |
Semliki Forest virus vectors: versatile tools for efficient large-scale expression of membrane receptors |
Kenneth Lundstrom |
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Abstract
One of the prerequisites for success in structural biology is to have access to large quantities of the protein of interest to enable purification and crystallization and furthermore to carry out high-resolution structural analysis. It is well known that only rarely, as in the case of rhodopsin, the protein concentration in native tissue is high enough to allow direct purification of material for structural studies. Particularly, transmembrane receptors are expressed at a rather low density and so far, among seven transmembrane receptors, only bacteriorhodopsin [1] and bovine rhodopsin [2, 3] have been successfully purified, crystallized and high-resolution structures resolved. There is, however, an enormous interest in the structural biology of receptors belonging to the family of G-protein coupled receptors (GPCRs) because many of these are involved in neurotransmission and important signal transduction events specifically in nerve cells. For this reason, GPCRs are the target molecules for intensive research to develop novel drugs for many central nervous system disorders including anxiety, depression and memory dysfunction.
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| 13 |
G protein-coupled receptor expression in , |
Ann M. Winter-Vann,Lynell Martinez,Cynthia Bartus,Agata Levay,George J. Turner |
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Abstract
A fundamental problem in the study of transmembrane proteins is the availability of protein, in the quantities required for detailed biochemical and biophysical characterization [see reviews 1,2]. Atomic resolution structures have solved for a handful of membrane proteins, including photoreaction centers [3–6], prostaglandin H2 synthase [7], porins of various species [8,9], cytochrome . oxidase [10], bacteriorhodopsin [11,12] a potassium channel [13], and bovine rhodopsin [14]. The structural characterization of these proteins was achieved, in part, because they were naturally available at very high expression levels.
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| 14 |
Magnetic resonance microscopy for studying the development of chicken and mouse embryos |
Robert E. Poelmann,Bianca Hogers,Huub J. M. de Groot,Cees Erkelens,Dieter Gross,Adriana C. Gittenberger-de Groot |
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Abstract
In this new era of transgenic mouse models, the need to evaluate the effects of gene manipulation during embryonic development is increasing. Traditional embryological studies are invasive, sacrificing embryos before processing in order to reveal specific information like morphology, histology, antigen distribution, gene expression patterns, or physiological parameters. Each objective requires a specific method, excluding the use of one specimen for multiple questions, while for temporal information each method has to be repeated on several specimens during development. The non-invasive character of magnetic resonance microscopy (MRM) allows the study of subsequent stages of normal development in a single embryo . over extended periods. In addition, MRM offers the possibility of studying the onset and course of a malformation during development. MRM has proven to be a powerful tool for fixed embryos [1] and living chicken embryos . [2]. Recently, Smith and coworkers [3] managed to visualize and follow living rat embryos . in a 2.0T MR microscope by a 3D projection encoding technique with a total scanning time of 27 min The objectives of the present study are to visualize fixed chicken embryos and living mouse embryos . Imaging of the embryo requires very high resolution in combination with excellent contrast. To achieve this, we used moderate to ultra high magnetic fields of 7.0 and 17.6T for the chicken material and 7.0T for the mouse embryos . and explored various fast imaging sequences. Fast imaging is necessary to avoid artifacts from embryonic movements that cannot be controlled by the researcher.
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| 15 |
MAS NMR on a uniformly [,C, ,N] labeled LH2 light-harvesting complex from , 10050 at ultra-high magnetic fields |
T. A. Egorova-Zachernyuk,J. Hollander,N. Fraser,P. Gast,A. J. Hoff,R. Cogdell,H. J. M. de Groot,M. Baldus |
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Abstract
Solid State Nuclear Magnetic resonance (SSNMR) spectroscopy is considered to be one of the tools for structure determinations of membrane proteins, and this technique, along with X-ray crystallography, will play an important role in structural genomics projects. The goal of structural genomics is the determination of the 3-D structure of all human proteins or of the complete sets of proteins in particular functional classes, such as enzymes or cell-surface receptors. As of today, 19 different structures of polytopic membrane proteins from inner membranes of bacteria and mitochondria and from eukaryotic membranes, 16 structures of membrane proteins from the outer membrane of gram negative bacteria and related membrane proteins, and 4 structures of the monotopic membrane proteins that are only inserted into the membrane have been determined by crystallographic methods .. At the same time, about 2000 structures of water soluble proteins have been determined. SS NMR is a tool for structure determination of the membrane proteins that can not be crystallized and for the structure-functional studies of the membrane proteins of known structure. Within this context it is important to get assignment data for solid state NMR studies.
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