scholarly journals Catalytically Active N -Heterocyclic Carbene Release from Single-Chain Nanoparticles Following a Thermolysis-Driven Unfolding Strategy

2019 ◽  
Vol 40 (15) ◽  
pp. 1970033
Author(s):  
Sofiem Garmendia ◽  
Stefan B. Lawrenson ◽  
Maria C. Arno ◽  
Rachel K. O'Reilly ◽  
Daniel Taton ◽  
...  
Keyword(s):  
Single Chain ◽  
Catalytically Active

scholarly journals Topology and quaternary structure of pro-sucrase/isomaltase and final-form sucrase/isomaltase

1986 ◽  
Vol 237 (2) ◽  
pp. 455-461 ◽  
Author(s):  
G M Cowell ◽  
J Tranum-Jensen ◽  
H Sjöström ◽  
O Norén
Keyword(s):  
Electron Microscopy ◽  
Quaternary Structure ◽  
Functional Organization ◽  
Enzyme Complex ◽  
Single Chain ◽  
Pancreatic Duct Ligation ◽  
Duct Ligation ◽  
Catalytically Active ◽  
Identical Series ◽  
Dimeric Model

Pig sucrase/isomaltase (EC 3.2.1.48/10) was purified from intestinal microvillar vesicles prepared from animals with and without pancreatic-duct ligation to obtain the single-chain pro form and the proteolytically cleaved final form respectively. The purified enzymes were re-incorporated into phosphatidylcholine vesicles and analysed by electron microscopy after negative staining. The two forms of the enzyme were observed as identical series of characteristic projected views that could be unified in a single dimeric model, containing two sucrase and two isomaltase units. This shows a homodimeric functional organization similar to that of other microvillar hydrolases. The bulk of the dimer was separated from the membrane by a maximal gap of 3.5 nm, representing a junctional segment connecting the intramembrane section of the anchor to the catalytically active domain of sucrase/isomaltase. The enzyme complex protrudes from the membrane for a distance of up to 17 nm. From charge-shift immunoelectrophoresic studies of hydrophilic prosucrase/isomaltase and from electron microscopy of reconstituted pro-sucrase/isomaltase, there was no evidence to suggest the presence of anchoring sequences between the sucrase and isomaltase subunits.

scholarly journals Catalytically Active Single-Chain Polymeric Nanoparticles: Exploring Their Functions in Complex Biological Media

2018 ◽  
Vol 140 (9) ◽  
pp. 3423-3433 ◽  
Author(s):  
Yiliu Liu ◽  
Sílvia Pujals ◽  
Patrick J. M. Stals ◽  
Thomas Paulöhrl ◽  
Stanislav I. Presolski ◽  
...  
Keyword(s):  
Polymeric Nanoparticles ◽  
Single Chain ◽  
Biological Media ◽  
Catalytically Active

scholarly journals Catalytically Active N ‐Heterocyclic Carbene Release from Single‐Chain Nanoparticles Following a Thermolysis‐Driven Unfolding Strategy

2019 ◽  
pp. 1900071 ◽  
Author(s):  
Sofiem Garmendia ◽  
Stefan B. Lawrenson ◽  
Maria C. Arno ◽  
Rachel K. O'Reilly ◽  
Daniel Taton ◽  
...  
Keyword(s):  
Single Chain ◽  
Catalytically Active

Pd(ii)–NHC coordination-driven formation of water-soluble catalytically active single chain nanoparticles

2018 ◽  
Vol 9 (23) ◽  
pp. 3199-3204 ◽  
Author(s):  
Romain Lambert ◽  
Anne-Laure Wirotius ◽  
Sofiem Garmendia ◽  
Pierre Berto ◽  
Joan Vignolle ◽  
...  
Keyword(s):  
Suzuki Coupling ◽  
Water Soluble ◽  
Intramolecular Coordination ◽  
Single Chain ◽  
Catalytically Active

Intramolecular coordination of a linear copolymer precursor yields single chain nanoparticles (SCNP's) consisting of Pd(ii)-NHC2 crosslinks and showing a beneficial SCNP effect when used for the Suzuki coupling in water.

Cryo-electron microscopy of two-dimensional crystals of reduced type B botulinum neurotoxin

1992 ◽  
Vol 50 (1) ◽  
pp. 530-531
Author(s):  
P. F. Flicker ◽  
V.S. Kulkarni ◽  
J. P. Robinson ◽  
G. Stubbs ◽  
B. R. DasGupta
Keyword(s):  
Disulfide Bonds ◽  
Clostridium Botulinum ◽  
Structural Changes ◽  
Two Dimensional ◽  
Type B ◽  
Single Chain ◽  
Muscle Paralysis ◽  
Cryo Electron Microscopy ◽  
Disulfide Linkages ◽  
Intracellular Action

Botulinum toxin is a potent neurotoxin produced by Clostridium botulinum. The toxin inhibits release of neurotransmitter, causing muscle paralysis. There are several serotypes, A to G, all of molecular weight about 150,000. The protein exists as a single chain or or as two chains, with two disulfide linkages. In a recent investigation on intracellular action of neurotoxins it was reported that type B neurotoxin can inhibit the release of Ca++-activated [3H] norepinephrine only if the disulfide bonds are reduced. In order to investigate possible structural changes in the toxin upon reduction of the disulfide bonds, we have prepared two-dimensional crystals of reduced type B neurotoxin. These two-dimensional crystals will be compared with those of the native (unreduced) type B toxin.

Fine structure and properties of defects in naturally occurring silicates and oxides

1990 ◽  
Vol 48 (4) ◽  
pp. 460-461
Author(s):  
David R. Veblen
Keyword(s):  
Chemical Reactions ◽  
High Resolution Electron Microscopy ◽  
Extended Defects ◽  
Single Chain ◽  
Naturally Occurring ◽  
Resolution Electron ◽  
Fine Structures ◽  
Image Simulations ◽  
Similar Crystal Structure

Extended defects and interfaces control many processes in rock-forming minerals, from chemical reactions to rock deformation. In many cases, it is not the average structure of a defect or interface that is most important, but rather the structure of defect terminations or offsets in an interface. One of the major thrusts of high-resolution electron microscopy in the earth sciences has been to identify the role of defect fine structures in reactions and to determine the structures of such features. This paper will review studies using HREM and image simulations to determine the structures of defects in silicate and oxide minerals and present several examples of the role of defects in mineral chemical reactions. In some cases, the geological occurrence can be used to constrain the diffusional properties of defects.The simplest reactions in minerals involve exsolution (precipitation) of one mineral from another with a similar crystal structure, and pyroxenes (single-chain silicates) provide a good example. Although conventional TEM studies have led to a basic understanding of this sort of phase separation in pyroxenes via spinodal decomposition or nucleation and growth, HREM has provided a much more detailed appreciation of the processes involved.

Elemental mass loss in silicate minerals during x-ray analysis

1990 ◽  
Vol 48 (4) ◽  
pp. 804-805
Author(s):  
P.E. Champness ◽  
R.W. Devenish
Keyword(s):  
Mass Loss ◽  
Current Density ◽  
Damage Mechanism ◽  
Beam Current ◽  
Single Chain ◽  
Plagioclase Feldspar ◽  
X Ray ◽  
Alkali Ions ◽  
Structural Order ◽  
Sheet Silicate

It has long been recognised that silicates can suffer extensive beam damage in electron-beam instruments. The predominant damage mechanism is radiolysis. For instance, damage in quartz, SiO2, results in loss of structural order without mass loss whereas feldspars (framework silicates containing Ca, Na, K) suffer loss of structural order with accompanying mass loss. In the latter case, the alkali ions, particularly Na, are found to migrate away from the area of the beam. The aim of the present study was to investigate the loss of various elements from the common silicate structures during electron irradiation at 100 kV over a range of current densities of 104 - 109 A m−2. (The current density is defined in terms of 50% of total current in the FWHM probe). The silicates so far ivestigated are:- olivine [(Mg, Fe)SiO4], a structure that has isolated Si-O tetrahedra, garnet [(Mg, Ca, Fe)3Al2Si3AO12 another silicate with isolated tetrahedra, pyroxene [-Ca(Mg, Fe)Si2O6 a single-chain silicate; mica [margarite, -Ca2Al4Si4Al4O2O(OH)4], a sheet silicate, and plagioclase feldspar [-NaCaAl3Si5O16]. Ion- thinned samples of each mineral were examined in a VG Microscopes UHV HB501 field- emission STEM. The beam current used was typically - 0.5 nA and the current density was varied by defocussing the electron probe. Energy-dispersive X-ray spectra were collected every 10 seconds for a total of 200 seconds using a Link Systems windowless detector. The thickness of the samples in the area of analysis was normally 50-150 nm.

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