Aggregation behavior of a series of structurally related single-chain amphiphiles. Structural effects on aggregate morphology as studied by electron microscopy

1984 ◽  
Vol 49 (17) ◽  
pp. 3088-3091 ◽  
Author(s):  
Frans J. A. Hundscheid ◽  
Jan B. F. N. Engberts
Keyword(s):  
Electron Microscopy ◽  
Aggregation Behavior ◽  
Structural Effects ◽  
Single Chain ◽  
Aggregate Morphology

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.

Amino-functionalized single-chain bolalipids: Synthesis and aggregation behavior of new basic building blocks

2010 ◽  
Vol 150 (1-3) ◽  
pp. 136-143 ◽  
Author(s):  
Simon Drescher ◽  
Gesche Graf ◽  
Gerd Hause ◽  
Bodo Dobner ◽  
Annette Meister
Keyword(s):  
Building Blocks ◽  
Aggregation Behavior ◽  
Single Chain

scholarly journals AFM and Electron Microscopy Study of the Unusual Aggregation Behavior of Metallosurfactants Based on Iron(II) Complexes with Bipyridine Ligands

Langmuir ◽  
2007 ◽  
Vol 23 (15) ◽  
pp. 7951-7957 ◽  
Author(s):  
Paula Garcia ◽  
Peter Eaton ◽  
Huub P. M. Geurts ◽  
Miguel Sousa ◽  
Paula Gameiro ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Microscopy Study ◽  
Electron Microscopy Study ◽  
Aggregation Behavior

scholarly journals Near-Atomic Resolution Structure of a Highly Neutralizing Fab Bound to Canine Parvovirus

2016 ◽  
Vol 90 (21) ◽  
pp. 9733-9742 ◽  
Author(s):  
Lindsey J. Organtini ◽  
Hyunwook Lee ◽  
Sho Iketani ◽  
Kai Huang ◽  
Robert E. Ashley ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Receptor Binding ◽  
Conformational Changes ◽  
De Novo ◽  
Mutational Analysis ◽  
Antibody Fragment ◽  
Canine Parvovirus ◽  
Single Chain ◽  
Cryo Electron Microscopy ◽  
Resolution Structure

ABSTRACT Canine parvovirus (CPV) is a highly contagious pathogen that causes severe disease in dogs and wildlife. Previously, a panel of neutralizing monoclonal antibodies (MAb) raised against CPV was characterized. An antibody fragment (Fab) of MAb E was found to neutralize the virus at low molar ratios. Using recent advances in cryo-electron microscopy (cryo-EM), we determined the structure of CPV in complex with Fab E to 4.1 Å resolution, which allowed de novo building of the Fab structure. The footprint identified was significantly different from the footprint obtained previously from models fitted into lower-resolution maps. Using single-chain variable fragments, we tested antibody residues that control capsid binding. The near-atomic structure also revealed that Fab binding had caused capsid destabilization in regions containing key residues conferring receptor binding and tropism, which suggests a mechanism for efficient virus neutralization by antibody. Furthermore, a general technical approach to solving the structures of small molecules is demonstrated, as binding the Fab to the capsid allowed us to determine the 50-kDa Fab structure by cryo-EM. IMPORTANCE Using cryo-electron microscopy and new direct electron detector technology, we have solved the 4 Å resolution structure of a Fab molecule bound to a picornavirus capsid. The Fab induced conformational changes in regions of the virus capsid that control receptor binding. The antibody footprint is markedly different from the previous one identified by using a 12 Å structure. This work emphasizes the need for a high-resolution structure to guide mutational analysis and cautions against relying on older low-resolution structures even though they were interpreted with the best methodology available at the time.

Formation of stable bilayer assemblies in water from single-chain amphiphiles. Relationship between the amphiphile structure and the aggregate morphology

1981 ◽  
Vol 103 (18) ◽  
pp. 5401-5413 ◽  
Author(s):  
Toyoki Kunitake ◽  
Yoshio Okahata ◽  
Masatsugu Shimomura ◽  
Shoichiro Yasunami ◽  
Kunihide Takarabe
Keyword(s):  
Single Chain ◽  
Aggregate Morphology

Structural Effects of Transition Metal Oxide Calcinations on Wurtzite Type Semiconductors That are Ferromagnetic at Room Temperature

2007 ◽  
Vol 999 ◽  
Author(s):  
Peter Moeck ◽  
Lori Noice ◽  
Chunfei Li ◽  
Amita Gupta ◽  
Rolf Erni ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Room Temperature ◽  
Weight Percent ◽  
First Principle ◽  
Structural Effects ◽  
X Ray ◽  
First Principle Calculations ◽  
Oxide Powders ◽  
Transmission Electron ◽  
Electron Energy Loss

AbstractGallium nitride powders and zinc oxide powders were each calcined with a few weight percent of copper oxide and/or magnesium oxide either in air or N2. Powder X-ray diffractometry, transmission electron microscopy, energy dispersive X-ray spectroscopy, and electron energy loss spectroscopy were performed in order to observe calcination induced structural effects on these wurtzite type semiconductors. We note that our earlier magnetic results on Cu doped GaN are qualitatively consistent with recent first principle calculations [Wu et al., Appl. Phys. Lett. 89 (2006) 62505].

Structural Effects of Anions and Cations on the Aggregation Behavior of Ionic Liquids in Aqueous Solutions

2008 ◽  
Vol 112 (51) ◽  
pp. 16682-16689 ◽  
Author(s):  
Huiyong Wang ◽  
Jianji Wang ◽  
Shibiao Zhang ◽  
Xiaopeng Xuan
Keyword(s):  
Ionic Liquids ◽  
Aqueous Solutions ◽  
Aggregation Behavior ◽  
Structural Effects ◽  
Anions And Cations

scholarly journals The Headgroup (A)Symmetry Strongly Determines the Aggregation Behavior of Single-Chain Phenylene-Modified Bolalipids and Their Miscibility with Classical Phospholipids

Langmuir ◽  
2014 ◽  
Vol 30 (31) ◽  
pp. 9273-9284 ◽  
Author(s):  
Simon Drescher ◽  
Bob-Dan Lechner ◽  
Vasil M. Garamus ◽  
László Almásy ◽  
Annette Meister ◽  
...  
Keyword(s):  
Aggregation Behavior ◽  
Single Chain
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