scholarly journals Positively charged bulk Au particles as an efficient catalyst for oxidation of styrene with molecular oxygen

2013 ◽  
Vol 49 (33) ◽  
pp. 3449 ◽  
Author(s):  
Liang Wang ◽  
Bingsen Zhang ◽  
Wei Zhang ◽  
Jian Zhang ◽  
Xionghou Gao ◽  
...  
2004 ◽  
Vol 2004 (5) ◽  
pp. 364-365 ◽  
Author(s):  
Mohammed M. Hashemi ◽  
Zahed Karimi-Jaberi ◽  
Dadkhoda Ghazanfari

Author(s):  
D.P. Bazett-Jones ◽  
F.P. Ottensmeyer

Dark field electron microscopy has been used for the study of the structure of individual macromolecules with a resolution to at least the 5Å level. The use of this technique has been extended to the investigation of structure of interacting molecules, particularly the interaction between DNA and fish protamine, a class of basic nuclear proteins of molecular weight 4,000 daltons.Protamine, which is synthesized during spermatogenesis, binds to chromatin, displaces the somatic histones and wraps up the DNA to fit into the small volume of the sperm head. It has been proposed that protamine, existing as an extended polypeptide, winds around the minor groove of the DNA double helix, with protamine's positively-charged arginines lining up with the negatively-charged phosphates of DNA. However, viewing protamine as an extended protein is inconsistent with the results obtained in our laboratory.


Author(s):  
D.P. Bazett-Jones ◽  
F.P. Ottensmeyer

It has been shown for some time that it is possible to obtain images of small unstained proteins, with a resolution of approximately 5Å using dark field electron microscopy (1,2). Applying this technique, we have observed a uniformity in size and shape of the 2-dimensional images of pure specimens of fish protamines (salmon, herring (clupeine, Y-l) and rainbow trout (Salmo irideus)). On the basis of these images, a model for the 3-dimensional structure of the fish protamines has been proposed (2).The known amino acid sequences of fish protamines show stretches of positively charged arginines, separated by regions of neutral amino acids (3). The proposed model for protamine structure (2) consists of an irregular, right-handed helix with the segments of adjacent arginines forming the loops of the coil.


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