Systematic structural analysis of a series of anion receptor complexes

CrystEngComm ◽  
2013 ◽  
Vol 15 (44) ◽  
pp. 9003 ◽  
Author(s):  
Isabelle L. Kirby ◽  
Mateusz B. Pitak ◽  
Marco Wenzel ◽  
Claire Wilson ◽  
Hazel A. Sparkes ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Anion Receptor ◽  
Receptor Complexes

scholarly journals Computational and Experimental Evidence of Emergent Equilibrium Isotope Effects in Anion Receptor Complexes

2017 ◽  
Vol 139 (11) ◽  
pp. 3962-3965 ◽  
Author(s):  
Blakely W. Tresca ◽  
Alexander C. Brueckner ◽  
Michael M. Haley ◽  
Paul H.-Y. Cheong ◽  
Darren W. Johnson
Keyword(s):  
Experimental Evidence ◽  
Isotope Effects ◽  
Anion Receptor ◽  
Receptor Complexes

scholarly journals Structural systematics of anion–receptor complexes: insights from electron-density distributions

2013 ◽  
Vol 69 (a1) ◽  
pp. s418-s418
Author(s):  
Isabelle L. Kirby ◽  
Mark Brightwell ◽  
Mateusz B. Pitak ◽  
Hazel A. Sparkes ◽  
Marco Wenzel ◽  
...  
Keyword(s):  
Electron Density ◽  
Anion Receptor ◽  
Density Distributions ◽  
Receptor Complexes

scholarly journals Systematic experimental charge density analysis of anion receptor complexes

2014 ◽  
Vol 16 (22) ◽  
pp. 10943-10958 ◽  
Author(s):  
Isabelle L. Kirby ◽  
Mark Brightwell ◽  
Mateusz B. Pitak ◽  
Claire Wilson ◽  
Simon J. Coles ◽  
...  
Keyword(s):  
Solid State ◽  
Charge Density ◽  
Anion Receptor ◽  
Binding Strength ◽  
Receptor Complexes ◽  
Density Analysis ◽  
Basic Anion ◽  
Experimental Charge Density ◽  
Resolution Study

The first systematic electronic resolution study of a series of urea-based anion receptor complexes is presented and shows the binding strength to be greater for more basic anion–receptor pairs in the solid state.

scholarly journals Reversible Intercalation of Fluoride-Anion Receptor Complexes in Graphite

2007 ◽  
Vol 154 (10) ◽  
pp. A929 ◽  
Author(s):  
William C. West ◽  
Jay F. Whitacre ◽  
Nicole Leifer ◽  
Steve Greenbaum ◽  
Marshall Smart ◽  
...  
Keyword(s):  
Fluoride Anion ◽  
Anion Receptor ◽  
Receptor Complexes

scholarly journals Structural systematics of anion–receptor complexes: insights from electron-density distributions

2013 ◽  
Vol 69 (a1) ◽  
pp. s93-s93
Author(s):  
Isabelle L. Kirby ◽  
Mark Brightwell ◽  
Mateusz B. Pitak ◽  
Hazel A. Sparkes ◽  
Marco Wenzel ◽  
...  
Keyword(s):  
Electron Density ◽  
Anion Receptor ◽  
Density Distributions ◽  
Receptor Complexes

scholarly journals Electron density distribution studies as a tool to explore the behaviour of thiourea-based anion receptors

CrystEngComm ◽  
2015 ◽  
Vol 17 (14) ◽  
pp. 2815-2826 ◽  
Author(s):  
Isabelle L. Kirby ◽  
Mateusz B. Pitak ◽  
Claire Wilson ◽  
Philip A. Gale ◽  
Simon J. Coles
Keyword(s):  
Density Distribution ◽  
Electron Density ◽  
Electron Density Distribution ◽  
Receptor Complex ◽  
Anion Receptors ◽  
Anion Receptor ◽  
Receptor Complexes ◽  
Distribution Studies ◽  
Substituted Urea

Building on previous studies of anion-receptor complexes based on a urea scaffold substituted symmetrically with electron-withdrawing nitro groups, the electron density distribution in an analogous thiourea receptor complex and the related asymmetrically substituted urea and thiourea receptors are described.

Structural analysis of the surface-layer protein of spirillum serpens by high-resolution electron microscopy

1983 ◽  
Vol 41 ◽  
pp. 738-739
Author(s):  
W. H. Wu ◽  
R. M. Glaeser
Keyword(s):  
Electron Microscopy ◽  
Surface Layer ◽  
Structural Analysis ◽  
High Resolution ◽  
Low Dose ◽  
High Resolution Electron Microscopy ◽  
Optical Diffraction ◽  
Surface Layer Protein ◽  
Morphological Unit ◽  
Resolution Electron

Spirillum serpens possesses a surface layer protein which exhibits a regular hexagonal packing of the morphological subunits. A morphological model of the structure of the protein has been proposed at a resolution of about 25 Å, in which the morphological unit might be described as having the appearance of a flared-out, hollow cylinder with six ÅspokesÅ at the flared end. In order to understand the detailed association of the macromolecules, it is necessary to do a high resolution structural analysis. Large, single layered arrays of the surface layer protein have been obtained for this purpose by means of extensive heating in high CaCl2, a procedure derived from that of Buckmire and Murray. Low dose, low temperature electron microscopy has been applied to the large arrays.As a first step, the samples were negatively stained with neutralized phosphotungstic acid, and the specimens were imaged at 40,000 magnification by use of a high resolution cold stage on a JE0L 100B. Low dose images were recorded with exposures of 7-9 electrons/Å2. The micrographs obtained (Fig. 1) were examined by use of optical diffraction (Fig. 2) to tell what areas were especially well ordered.

RNA polymerase: Preparation and structural analysis of helical polymers

1984 ◽  
Vol 42 ◽  
pp. 152-153
Author(s):  
E. Loren Buhle ◽  
Pamela Rew ◽  
Ueli Aebi
Keyword(s):  
Structural Analysis ◽  
Rna Polymerase ◽  
Molecular Level ◽  
X Ray Diffraction ◽  
Helical Polymers ◽  
X Ray ◽  
E Coli ◽  
The Past ◽  
Ordered Arrays ◽  
Low Ionic Strength

While DNA-dependent RNA polymerase represents one of the key enzymes involved in transcription and ultimately in gene expression in procaryotic and eucaryotic cells, little progress has been made towards elucidation of its 3-D structure at the molecular level over the past few years. This is mainly because to date no 3-D crystals suitable for X-ray diffraction analysis have been obtained with this rather large (MW ~500 kd) multi-subunit (α2ββ'ζ). As an alternative, we have been trying to form ordered arrays of RNA polymerase from E. coli suitable for structural analysis in the electron microscope combined with image processing. Here we report about helical polymers induced from holoenzyme (α2ββ'ζ) at low ionic strength with 5-7 mM MnCl2 (see Fig. 1a). The presence of the ζ-subunit (MW 86 kd) is required to form these polymers, since the core enzyme (α2ββ') does fail to assemble into such structures under these conditions.

The relationship of IGE receptor topography to signaling activity in RBL-2H3 mast cells

1991 ◽  
Vol 49 ◽  
pp. 236-237
Author(s):  
J.R. Pfeiffer ◽  
J.C. Seagrave ◽  
C. Wofsy ◽  
J.M. Oliver
Keyword(s):  
Mast Cells ◽  
Protein A ◽  
Scattered Electron ◽  
Ige Receptor ◽  
Receptor Complexes ◽  
Ige Binding ◽  
Electron Imaging ◽  
Small Clusters ◽  
Relationship Of ◽  
The Relationship

In RBL-2H3 rat leukemic mast cells, crosslinking IgE-receptor complexes with anti-IgE antibody leads to degranulation. Receptor crosslinking also stimulates the redistribution of receptors on the cell surface, a process that can be observed by labeling the anti-IgE with 15 nm protein A-gold particles as described in Stump et al. (1989), followed by back-scattered electron imaging (BEI) in the scanning electron microscope. We report that anti-IgE binding stimulates the redistribution of IgE-receptor complexes at 37“C from a dispersed topography (singlets and doublets; S/D) to distributions dominated sequentially by short chains, small clusters and large aggregates of crosslinked receptors. These patterns can be observed (Figure 1), quantified (Figure 2) and analyzed statistically. Cells incubated with 1 μg/ml anti-IgE, a concentration that stimulates maximum net secretion, redistribute receptors as far as chains and small clusters during a 15 min incubation period. At 3 and 10 μg/ml anti-IgE, net secretion is reduced and the majority of receptors redistribute rapidly into clusters and large aggregates.

The distribution of antigen on the surface of RBL-2H3 rat basophilic leukemia cells observed by back-scattered electron imaging

1986 ◽  
Vol 44 ◽  
pp. 274-275
Author(s):  
R.F. Stump ◽  
J.R. Pfeiffer ◽  
JC. Seagrave ◽  
D. Huskisson ◽  
J.M. Oliver
Keyword(s):  
Cell Surface ◽  
Dynamic Properties ◽  
Leukemia Cells ◽  
Antigen Binding ◽  
Scattered Electron ◽  
Ige Receptor ◽  
Receptor Complexes ◽  
Rat Basophilic Leukemia Cells ◽  
Electron Imaging ◽  
Basophilic Leukemia

In RBL-2H3 rat basophilic leukemia cells, antigen binding to cell surface IgE-receptor complexes stimulates the release of inflammatory mediators and initiates a series of membrane and cytoskeletal events including a transformation of the cell surface from a microvillous to a lamellar topography. It is likely that dynamic properties of the IgE receptor contribute to the activation of these responses. Fewtrell and Metzger have established that limited crosslinking of IgE-receptor complexes is essential to trigger secretion. In addition, Baird and colleagues have reported that antigen binding causes a rapid immobilization of IgE-receptor complexes, and we have demonstrated an apparent increase with time in the affinity of IgE-receptor complexes for antigen.

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