Quantitative Analysis of the Self-Assembly Strategies of Intermediate Filaments from Tetrameric Vimentin

2012 ◽  
Vol 9 (3) ◽  
pp. 885-898 ◽  
Author(s):  
E. Czeizler ◽  
A. Mizera ◽  
E. Czeizler ◽  
R-J Back ◽  
J. E. Eriksson ◽  
...  
Keyword(s):  
Quantitative Analysis ◽  
Intermediate Filaments ◽  
Self Assembly ◽  
The Self

Neutron Reflectometry of Membrane Protein Assemblies at the Solid/Liquid Interface

2005 ◽  
Vol 58 (9) ◽  
pp. 674 ◽  
Author(s):  
Stephen A. Holt ◽  
Jeremy H. Lakey ◽  
Sofian M. Daud ◽  
Neil Keegan
Keyword(s):  
Quantitative Analysis ◽  
Membrane Protein ◽  
Self Assembly ◽  
Neutron Reflectometry ◽  
The Self ◽  
Water Molecules ◽  
Gold Substrate ◽  
Protein Assemblies ◽  
Solid Liquid Interface ◽  
Solid Liquid

Neutron reflectometry has been used to study the self-assembly of a membrane protein, OmpF, onto a gold-coated silicon substrate from solution. OmpF associates into trimers and has been modified so that each trimer binds to the gold substrate through cysteine residues. Quantitative analysis of the data revealed that 12% of the surface was covered by the oriented protein with 27600 water molecules surrounding each trimer.

Quantitative Analysis of the Self-Assembly Process of a Pd12 L24 Coordination Sphere

2017 ◽  
Vol 12 (24) ◽  
pp. 3203-3207 ◽  
Author(s):  
Shumpei Kai ◽  
Taro Shigeta ◽  
Tatsuo Kojima ◽  
Shuichi Hiraoka
Keyword(s):  
Quantitative Analysis ◽  
Coordination Sphere ◽  
Self Assembly ◽  
The Self ◽  
Assembly Process

scholarly journals Reconstitution of intermediate filaments from a higher plant

1989 ◽  
Vol 261 (2) ◽  
pp. 679-682 ◽  
Author(s):  
A J Hargreaves ◽  
K C Goodbody ◽  
C W Lloyd
Keyword(s):  
Intermediate Filaments ◽  
Self Assembly ◽  
Insoluble Fraction ◽  
Cross Reactivity ◽  
The Self ◽  
Suspension Cells ◽  
Higher Plant ◽  
Daucus Carota L ◽  
Molecular Masses ◽  
10 Nm Filaments

Immunological studies have shown that plants contain intermediate-filament antigens, but it is not known whether these proteins are capable in themselves of forming filaments. To address this problem, a detergent-resistant and high-salt-insoluble fraction from carrot (Daucus carota L.) suspension cells was solubilized with 9 M-urea and then subjected to a two-step dialysis procedure, devised for the reconstitution of animal intermediate filaments. This induced the self-assembly of 10 nm filaments and large bundles of filaments. The predominant components of reconstituted material were polypeptides with apparent molecular masses between 58 and 62 kDa. These polypeptides immunoblotted with two monoclonal antibodies known to show broad cross-reactivity with intermediate filaments across the phylogenetic spectrum. This establishes that the antigens are able to self-assemble into intermediate-sized filaments.

The Nature of Rapidly Extracted Phycocyanin from the Blue-Green Alga Plectonema Boryanum

1971 ◽  
Vol 29 ◽  
pp. 366-367
Author(s):  
M. Kessel ◽  
R. MacColl
Keyword(s):  
Self Assembly ◽  
Analytical Ultracentrifugation ◽  
Uranyl Acetate ◽  
The Self ◽  
Major Protein ◽  
Subunit Structure ◽  
Blue Green Alga ◽  
Thin Sections ◽  
Blue Green Algae ◽  
Cacodylate Buffer

The major protein of the blue-green algae is the biliprotein, C-phycocyanin (Amax = 620 nm), which is presumed to exist in the cell in the form of distinct aggregates called phycobilisomes. The self-assembly of C-phycocyanin from monomer to hexamer has been extensively studied, but the proposed next step in the assembly of a phycobilisome, the formation of 19s subunits, is completely unknown. We have used electron microscopy and analytical ultracentrifugation in combination with a method for rapid and gentle extraction of phycocyanin to study its subunit structure and assembly.To establish the existence of phycobilisomes, cells of P. boryanum in the log phase of growth, growing at a light intensity of 200 foot candles, were fixed in 2% glutaraldehyde in 0.1M cacodylate buffer, pH 7.0, for 3 hours at 4°C. The cells were post-fixed in 1% OsO4 in the same buffer overnight. Material was stained for 1 hour in uranyl acetate (1%), dehydrated and embedded in araldite and examined in thin sections.

Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

1992 ◽  
Vol 50 (1) ◽  
pp. 712-713
Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh
Keyword(s):  
Alkaline Phosphatase ◽  
Bacillus Licheniformis ◽  
Self Assembly ◽  
Gel Electrophoresis ◽  
Culture Supernatant ◽  
Regular Structure ◽  
The Self ◽  
Cellular Distribution ◽  
Structural Protein ◽  
Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

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