Effects of monopropanediamino-β-cyclodextrin on the denaturation process of the hybrid protein BlaPChBD

2011 ◽  
Vol 1814 (9) ◽  
pp. 1146-1153 ◽  
Author(s):  
Marylène Vandevenne ◽  
Gilles Gaspard ◽  
El Mustapha Belgsir ◽  
Manilduth Ramnath ◽  
Yves Cenatiempo ◽  
...  
Nanomaterials ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 1332
Author(s):  
Armando Hernandez-Garcia

Proteins and DNA exhibit key physical chemical properties that make them advantageous for building nanostructures with outstanding features. Both DNA and protein nanotechnology have growth notably and proved to be fertile disciplines. The combination of both types of nanotechnologies is helpful to overcome the individual weaknesses and limitations of each one, paving the way for the continuing diversification of structural nanotechnologies. Recent studies have implemented a synergistic combination of both biomolecules to assemble unique and sophisticate protein–DNA nanostructures. These hybrid nanostructures are highly programmable and display remarkable features that create new opportunities to build on the nanoscale. This review focuses on the strategies deployed to create hybrid protein–DNA nanostructures. Here, we discuss strategies such as polymerization, spatial directing and organizing, coating, and rigidizing or folding DNA into particular shapes or moving parts. The enrichment of structural DNA nanotechnology by incorporating protein nanotechnology has been clearly demonstrated and still shows a large potential to create useful and advanced materials with cell-like properties or dynamic systems. It can be expected that structural protein–DNA nanotechnology will open new avenues in the fabrication of nanoassemblies with unique functional applications and enrich the toolbox of bionanotechnology.


Author(s):  
Tomas R. Ines ◽  
Francisco J. Cisneros ◽  
Angel Goni ◽  
Juan Castellanos

1990 ◽  
Vol 589 (1 Biochemical E) ◽  
pp. 139-147 ◽  
Author(s):  
GEORGE GEORGIOU ◽  
FRANÇOIS BANEYX
Keyword(s):  

1990 ◽  
Vol 10 (6) ◽  
pp. 3163-3173
Author(s):  
C A Kaiser ◽  
D Botstein

Three randomly derived sequences that can substitute for the signal peptide of Saccharomyces cerevisiae invertase were tested for the efficiency with which they can translocate invertase or beta-galactosidase into the endoplasmic reticulum. The rate of translocation, as measured by glycosylation, was estimated in pulse-chase experiments to be less than 6 min. When fused to beta-galactosidase, these peptides, like the normal invertase signal sequence, direct the hybrid protein to a perinuclear region, consistent with localization to the endoplasmic reticulum. The diversity of function of random peptides was studied further by immunofluorescence localization of proteins fused to 28 random sequences: 4 directed the hybrid to the endoplasmic reticulum, 3 directed it to the mitochondria, and 1 directed it to the nucleus.


1986 ◽  
Vol 159 (3) ◽  
pp. 605-609 ◽  
Author(s):  
Isabella CRENON ◽  
Daniel LADANT ◽  
Nicole GUISO ◽  
Anne-Marie GILLES ◽  
Octavian BARZU

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