scholarly journals Nanoplasmonic ruler to measure lipid vesicle deformation

2016 ◽  
Vol 52 (1) ◽  
pp. 76-79 ◽  
Author(s):  
Joshua A. Jackman ◽  
Barbora Špačková ◽  
Eric Linardy ◽  
Min Chul Kim ◽  
Bo Kyeong Yoon ◽  
...  
Keyword(s):  
Direct Evidence ◽  
Lipid Vesicle ◽  
Membrane Tension ◽  
Vesicle Adsorption

A nanoplasmonic ruler measures vesicle deformation and provides direct evidence to support membrane tension-based models of vesicle adsorption and rupture.

Simulations of Lipid Vesicle Adsorption for Different Lipid Mixtures

Langmuir ◽  
2008 ◽  
Vol 24 (8) ◽  
pp. 4077-4091 ◽  
Author(s):  
Kristian Dimitrievski ◽  
Bengt Kasemo
Keyword(s):  
Lipid Vesicle ◽  
Lipid Mixtures ◽  
Vesicle Adsorption

Influence of Lipid-Bilayer-Associated Molecules on Lipid-Vesicle Adsorption

Langmuir ◽  
2010 ◽  
Vol 26 (8) ◽  
pp. 5706-5714 ◽  
Author(s):  
Kristian Dimitrievski
Keyword(s):  
Lipid Bilayer ◽  
Lipid Vesicle ◽  
Vesicle Adsorption

scholarly journals Lipid vesicle adsorption versus formation of planar bilayers on solid surfaces

1995 ◽  
Vol 69 (4) ◽  
pp. 1447-1455 ◽  
Author(s):  
P. Nollert ◽  
H. Kiefer ◽  
F. Jähnig
Keyword(s):  
Solid Surfaces ◽  
Lipid Vesicle ◽  
Planar Bilayers ◽  
Vesicle Adsorption

The Immuno-Electron Microscopic Localization of the Mo-Fe Protein Component of Nitrogenase in Cells of Azotobacter Vinelandii

1973 ◽  
Vol 31 ◽  
pp. 574-575
Author(s):  
J. T. Stasny ◽  
R. C. Burns ◽  
R. W. F. Hardy
Keyword(s):  
Cellular Localization ◽  
Direct Evidence ◽  
Azotobacter Vinelandii ◽  
Intracellular Localization ◽  
Protein Component ◽  
Electron Microscopic ◽  
Thin Sections ◽  
Fe Protein ◽  
Intracytoplasmic Membranes

Structure-functlon studies of biological N2-fixation have correlated the presence of the enzyme nitrogenase with increased numbers of intracytoplasmic membranes in Azotobacter. However no direct evidence has been provided for the internal cellular localization of any nitrogenase. Recent advances concerned with the crystallizatiorTand the electron microscopic characterization of the Mo-Fe protein component of Azotobacter nitrogenase, prompted the use of this purified protein to obtain antibodies (Ab) to be conjugated to electron dense markers for the intracellular localization of the protein by electron microscopy. The present study describes the use of ferritin conjugated to goat antitMo-Fe protein immunoglobulin (IgG) and the observations following its topical application to thin sections of N2-grown Azotobacter.

Structural similarity of ribosomes from E. coli and A. salina

1978 ◽  
Vol 36 (2) ◽  
pp. 242-243
Author(s):  
M. Boublik ◽  
R.M. Wydro ◽  
W. Hellmann ◽  
F. Jenkins
Keyword(s):  
Ribosomal Proteins ◽  
Direct Evidence ◽  
Structural Similarity ◽  
Carbon Support ◽  
Artemia Salina ◽  
Uranyl Acetate ◽  
Biological Assays ◽  
E Coli ◽  
And Function ◽  
Fine Carbon

Ribosomes are ribonucleoprotein particles necessary for processing the genetic information of mRNA into proteins. Analogy in composition and function of ribosomes from diverse species, established by biochemical and biological assays, implies their structural similarity. Direct evidence obtained by electron microscopy seems to be of increasing relevance in understanding the structure of ribosomes and the mechanism of their role in protein synthesis.The extent of the structural homology between prokaryotic and eukaryotic ribosomes has been studied on ribosomes of Escherichia coli (E.c.) and Artemia salina (A.s.). Despite the established differences in size and in the amount and proportion of ribosomal proteins and RNAs both types of ribosomes show an overall similarity. The monosomes (stained with 0.5% aqueous uranyl acetate and deposited on a fine carbon support) appear in the electron micrographs as round particles with a diameter of approximately 225Å for the 70S E.c. (Fig. 1) and 260Å for the 80S A.s. monosome (Fig. 2).

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