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Journal ArticleDOI

Bicelles: a model membrane system for all seasons?

15 Oct 1998-Structure (Elsevier)-Vol. 6, Iss: 10, pp 1227-1234
TL;DR: The support of the National Science Foundation (MCB-9513357), National institutes of Health (GM47485), and the American Heart Association (through an Established Investigatorship to CS) is gratefully acknowledged.
About: This article is published in Structure.The article was published on 1998-10-15 and is currently open access. It has received 322 citations till now.
Citations
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Journal ArticleDOI
TL;DR: This review will concentrate on the methods currently available for efficient reconstitution and solubilization of membrane proteins through the use of detergent micelles, mixed lipid/detergent micella and bicelles or liposomes and the role that lipids can play in stabilizing the proteins.

1,270 citations

Journal ArticleDOI
TL;DR: Structural analysis by solid-state NMR spectroscopy and other biophysical techniques indicates that these peptide antibiotics strongly interact with lipid membranes, which contrasts the transmembrane orientations observed for alamethicin or gramicidin A.

482 citations

Journal ArticleDOI
TL;DR: Within its relatively short history, nuclear magnetic resonance (NMR) spectroscopy has managed to play an important role in the characterization of biomolecular structure, however, the methods on which most of this characterization has been based, Nuclear Overhauser Effect measurements for short-range distance constraints and scalar couplings measurements for torsional constraints, have limitations.
Abstract: 2. Theoretical treatment of dipolar interactions 376 2.1 Anisotropic interactions as probes of macromolecular structure and dynamics 376 2.1.1 The dipolar interaction 376 2.1.2 Averaging in the solution state 377 2.2 Ordering of a rigid body 377 2.2.1 The Saupe order tensor 378 2.2.2 Orientational probability distribution function 380 2.2.3 The generalized degree of order 380 2.3 Molecular structure and internal dynamics 381

418 citations


Cites background or methods from "Bicelles: a model membrane system f..."

  • ...Some of the key limitations of the original bicelle media are lack of tolerance to a wide range of biologically relevant conditions, and a limited life span (Ottiger & Bax, 1998; Sanders & Prosser, 1998)....

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  • ...Ordered bicelle domains exist only over well-defined limits of composition, temperature, and presumably pressure (Sanders et al. 1994; Sanders & Prosser, 1998)....

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  • ...Bicelles have thus far been the most widely used aligning media in high resolution NMR applications (Sanders & Prosser, 1998)....

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  • ...Both the number of lipids in the bicelle and the cooperative alignment of bicelles in the liquid crystal domain amplify the magnitude of the anisotropy tensor and result in very high levels of order, even at moderate field strengths (Sanders & Prosser, 1998)....

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Journal ArticleDOI
TL;DR: One-dimensional dipolar waves are an extension of two-dimensional PISA (polarity index slant angle) wheels that map protein structures in NMR spectra of both weakly and completely aligned samples, and represent a convergence of solid-state and solution NMR approaches to structure determination.
Abstract: Much of postgenomic biochemistry and all of structural biology are based on the premise that the starting point for both understanding specific biochemical processes, such as affinity, reactivity, or transport, and surveying proteomes is determining the three-dimensional structures of proteins. The two well-established methods for structure determination are highly effective when applied to samples of soluble globular proteins and their complexes: witness the enormous growth of the Protein Data Bank.1 However, the vast majority of biological functions are carried out by proteins associated with supramolecular assemblies, whose samples are problematic for both X-ray crystallography and solution NMR spectroscopy, since they are generally difficult to crystallize and do not reorient rapidly even when soluble. The examples of proteins in supramolecular assemblies whose structures have been determined with atomic resolution are exceptional and highlight the importance of developing new methods of experimental protein structure determination. The essential goals of modern structural biology are to have the capability to select proteins for study based on their biological functions and to perform genuinely unbiased surveys of proteomes unfettered by considerations of the solubility, aggregation state, or other physical properties of the polypeptides. NMR spectroscopy has the potential to accomplish these goals, since it can be applied to molecules in all physical states, including the liquid crystalline environments provided by the lipids associated with membrane proteins. Determining the atomic resolution structures of membrane proteins is of particular interest in contemporary structural biology.2 Helical membrane proteins constitute one-third of the expressed proteins encoded in a genome.3,4 Furthermore, many drugs have membrane-bound proteins as their receptors, and mutations in membrane proteins result in human diseases. They also provide daunting technical challenges for all methods of protein structure determination, including NMR spectroscopy.5

410 citations

Journal ArticleDOI
TL;DR: In this paper, a method for crystallizing membrane proteins from a bicelle forming lipid/detergent mixture was presented, which is flexible and simple to use and yields a new bR crystal form.

346 citations

References
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Journal ArticleDOI
07 Nov 1997-Science
TL;DR: The approach promises to improve the accuracy of structures determined by NMR, and extend the size limit, and distances and angles derived from dipolar couplings in human ubiquitin are in excellent agreement with its crystal structure.
Abstract: In isotropic solution, internuclear dipolar couplings average to zero as a result of rotational diffusion. By dissolving macromolecules in a dilute aqueous nematic discotic liquid-crystalline medium containing widely spaced magnetically oriented particles, a tunable degree of solute alignment with the magnetic field can be created while retaining the high resolution and sensitivity of the regular isotropic nuclear magnetic resonance (NMR) spectrum. Dipolar couplings between1H-1H, 1H-13C,1H-15N, and 13C-13C pairs in such an oriented macromolecule no longer average to zero, and are readily measured. Distances and angles derived from dipolar couplings in human ubiquitin are in excellent agreement with its crystal structure. The approach promises to improve the accuracy of structures determined by NMR, and extend the size limit.

1,634 citations


"Bicelles: a model membrane system f..." refers background in this paper

  • ...Variations in the scaling of order for water-soluble biomolecules can be achieved simply by varying the percentage of water in a bicellar sample [6,7,26]....

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  • ...Tjandra and Bax have recently used bicelles [6,7] to achieve a desired degree of sample alignment of ubiquitin and other water-soluble biomolecules and complexes....

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  • ...There is now considerable NMR data [5–7] to suggest that CHAPSO–DMPC and DHPC–DMPC bicelles do indeed provide a generally inert environment for water soluble proteins....

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  • ...Indeed, Tjandra and Bax were able to observe a few long-range 1H–1H dipolar couplings in their original study [6,7], foretelling what promises to be a bounteous future....

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  • ...The advantage of bicelles to free molecule alignment of water soluble species is that the net degree of orientation achievable at reasonable field strength is much higher, making detection and measurement of dipolar couplings and CSA much easier [6,7]....

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Journal ArticleDOI
TL;DR: In this paper, the authors present a review of the structure and dynamics of polymers using multidimensional NMR and derive a determination of order in polymers by multi-dimensional NMR.
Abstract: Introduction. Principles of NMR of Organic Solids. High-Resolution NMR Techniques for Solids. Fourier Theory for 1D and 2D NMR. Short Review of Structure and Dynamics of Solid Polymers. Multidimensional Separation and Correlation. Polymer Dynamics: Multidimensional Exchange Experiments. Multidimensional Exchange NMR Above the Glass Transition. Multidimensional Spectra, Correlation Functions, and Stochastic Processes. Time-Domain Signals for Multidimensional Spectra. Multidimensional Exchange Spectra: Simulations, Models, Angle Distributions. Determination of Order in Polymers by Multidimensional NMR. Domain Sizes and Internuclear Distances from Spin Diffusion and Dipolar Couplings. Appendices. Chapter References. Index.

1,497 citations

Journal ArticleDOI
06 Jul 1989-Nature
TL;DR: Both in Britain and the United States the public says it is more interested in science than (for example, sport), but public knowledge of science gives less cause for gratification.
Abstract: Both in Britain and the United States the public says it is more interested in science than (for example) sport. Public knowledge of science gives less cause for gratification.

1,102 citations

Journal ArticleDOI
TL;DR: The thickness of the lipid bilayer in vesicles made of pure phosphatidylcholines, with acyl chain lengths ranging from 10 to 24 carbons, has been determined by analysis of continuous X-ray scattering data from vesicle pellets at temperatures above the lipid phase transition temperature.

752 citations


"Bicelles: a model membrane system f..." refers background in this paper

  • ...An attempt has been made to draw the bicelles approximately to scale on the basis of the known dimensions of α helices, liquid crystalline phosphatidylcholine molecules [55], the thickness of DMPC bilayers [55] and the probable disc diameter of bicelles [39,40]....

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Journal ArticleDOI
TL;DR: The measurement of dipolar contributions to the splitting of 15N resonances of 1H-15N amide pairs in multidimensional high-field NMR spectra of field-oriented cyanometmyoglobin is reported and implications as an additional source of information for protein structure determination in solution are discussed.
Abstract: The measurement of dipolar contributions to the splitting of 15N resonances of 1H-15N amide pairs in multidimensional high-field NMR spectra of field-oriented cyanometmyoglobin is reported. The splittings appear as small field-dependent perturbations of normal scalar couplings. Assignment of more than 90 resonances to specific sequential sites in the protein allows correlation of the dipolar contributions with predictions based on the known susceptibility and known structure of the protein. Implications as an additional source of information for protein structure determination in solution are discussed.

750 citations