Electrochemical Determination of Nucleic Acid Diffusion Coefficients through Noncovalent Association of a Redox-Active Probe

1995 ◽  
Vol 99 (30) ◽  
pp. 11757-11763 ◽  
Author(s):  
Thomas W. Welch ◽  
Amanda H. Corbett ◽  
H. Holden Thorp
Keyword(s):  
Nucleic Acid ◽  
Diffusion Coefficients ◽  
Electrochemical Determination ◽  
Acid Diffusion ◽  
Redox Active ◽  
Active Probe

Electrochemical Determination of Hg2+Using Electrodes Modified with Peptide Nucleic Acid

2016 ◽  
Vol 163 (14) ◽  
pp. B667-B672 ◽  
Author(s):  
Agnieszka Bala ◽  
Krzysztof Zalewski ◽  
Łukasz Górski
Keyword(s):  
Nucleic Acid ◽  
Peptide Nucleic Acid ◽  
Electrochemical Determination

Electrochemical Determination of Diffusion Coefficients of Iron (II) Ions in Chloride Melts at 700-750°C

2007 ◽  
Vol 47 (3-4) ◽  
pp. 409-414 ◽  
Author(s):  
Alex Lugovskoy ◽  
Michael Zinigrad ◽  
Doron Aurbach
Keyword(s):  
Diffusion Coefficients ◽  
Electrochemical Determination ◽  
Chloride Melts

The electrochemical determination of oxygen ion diffusion coefficients in La0.50Sr0.50CoO3−y

1978 ◽  
Vol 88 (3) ◽  
pp. 353-361 ◽  
Author(s):  
F.R. Van Buren ◽  
G.H.J. Broers ◽  
A.J. Bouman ◽  
C. Boesveld
Keyword(s):  
Diffusion Coefficients ◽  
Electrochemical Determination ◽  
Ion Diffusion ◽  
Oxygen Ion ◽  
Oxygen Ion Diffusion

Electrochemical Determination of Oxidic Melt Diffusion Coefficients

2005 ◽  
Vol 26 (4) ◽  
pp. 1181-1192 ◽  
Author(s):  
K. Frolov ◽  
C. Journeau ◽  
P. Piluso ◽  
M. Duclot
Keyword(s):  
Diffusion Coefficients ◽  
Electrochemical Determination

scholarly journals Carbon ceramic microelectrodes modified with buckyballs for simultaneous determination of redox-active biomolecules

RSC Advances ◽  
2018 ◽  
Vol 8 (11) ◽  
pp. 5960-5966 ◽  
Author(s):  
Z. Omara Shastan ◽  
Hashwin V. S. Ganesh ◽  
Meissam Noroozifar ◽  
Kagan Kerman
Keyword(s):  
Ascorbic Acid ◽  
Uric Acid ◽  
Simultaneous Determination ◽  
Electrochemical Determination ◽  
Redox Active ◽  
Carbon Ceramic

In this report, simultaneous electrochemical determination of ascorbic acid (AA), dopamine (DA), uric acid (UA) and tryptophan (Trp) was achieved using buckyball-modified carbon ceramic microelectrodes (CCMEs).

Imaging of ribosomal RNA-protein interactions by dark-field STEM

1989 ◽  
Vol 47 ◽  
pp. 250-251
Author(s):  
M. Boublik ◽  
V. Mandiyan ◽  
S. Tumminia ◽  
J.F. Hainfeld ◽  
J.S. Wall
Keyword(s):  
Nucleic Acid ◽  
16S Rrna ◽  
Dark Field ◽  
Radius Of Gyration ◽  
Central Domain ◽  
The Core ◽  
16S Rna ◽  
30S Subunit ◽  
Core Particles

Success in protein-free deposition of native nucleic acid molecules from solutions of selected ionic conditions prompted attempts for high resolution imaging of nucleic acid interactions with proteins, not attainable by conventional EM. Since the nucleic acid molecules can be visualized in the dark-field STEM mode without contrasting by heavy atoms, the established linearity between scattering cross-section and molecular weight can be applied to the determination of their molecular mass (M) linear density (M/L), mass distribution and radius of gyration (RG). Determination of these parameters promotes electron microscopic imaging of biological macromolecules by STEM to a quantitative analytical level. This technique is applied to study the mechanism of 16S rRNA folding during the assembly process of the 30S ribosomal subunit of E. coli. The sequential addition of protein S4 which binds to the 5'end of the 16S rRNA and S8 and S15 which bind to the central domain of the molecule leads to a corresponding increase of mass and increased coiling of the 16S rRNA in the core particles. This increased compactness is evident from the decrease in RG values from 114Å to 91Å (in “ribosomal” buffer consisting of 10 mM Hepes pH 7.6, 60 mM KCl, 2 m Mg(OAc)2, 1 mM DTT). The binding of S20, S17 and S7 which interact with the 5'domain, the central domain and the 3'domain, respectively, continues the trend of mass increase. However, the RG values of the core particles exhibit a reverse trend, an increase to 108Å. In addition, the binding of S7 leads to the formation of a globular mass cluster with a diameter of about 115Å and a mass of ∽300 kDa. The rest of the mass, about 330 kDa, remains loosely coiled giving the particle a “medusa-like” appearance. These results provide direct evidence that 16S RNA undergoes significant structural reorganization during the 30S subunit assembly and show that its interactions with the six primary binding proteins are not sufficient for 16S rRNA coiling into particles resembling the native 30S subunit, contrary to what has been reported in the literature.

Sign in / Sign up

Export Citation Format

Share Document