Effect of Peptide Charge Distribution on the Structure and Kinetics of DNA Complex

2015 ◽  
Vol 48 (3) ◽  
pp. 756-763 ◽  
Author(s):  
Cuicui Su ◽  
Mingtian Zhao ◽  
Zhichao Zhu ◽  
Jihan Zhou ◽  
Hao Wen ◽  
...  
1998 ◽  
Vol 45 (1) ◽  
pp. 127-132 ◽  
Author(s):  
M Piestrzeniewicz ◽  
K Studzian ◽  
D Wilmańska ◽  
G Płucienniczak ◽  
M Gniazdowski

9-Aminoacridine carboxamide derivatives studied here form with DNA intercalative complexes which differ in the kinetics of dissociation. Inhibition of total RNA synthesis catalyzed by phage T7 and Escherichia coli DNA-dependent RNA polymerases correlates with the formation of slowly dissociating acridine-DNA complex of time constant of 0.4-2.3 s. Their effect on RNA synthesis is compared with other ligands which form with DNA stable complexes of different steric properties. T7 RNA polymerase is more sensitive to distamycin A and netropsin than the E. coli enzyme while less sensitive to actinomycin D. Actinomycin induces terminations in the transcript synthesized by T7 RNA polymerase. Despite low dissociation rates of DNA complexes with acridines and pyrrole antibiotics no drug dependent terminations are observed with these ligands.


Kinetic measurements have been made at 25 ° C on the halogenation of benzoylacetone, acetylacetone, ethyl acetoacetate, ethyl α-bromoacetoacetate and diethyl bromomalonate. A method is described for analyzing the kinetic data and obtaining the rates of substitution of successive halogen atoms without isolating the partly halogenated derivatives. The reaction velocities measured are all independent of the halogen concentration, and represent the rates of ionization of the ketonic substances in presence of basic catalysts. The results obtained conform in general to the regularities previously found for this type of reaction, but anomalies are found in some instances; these are related to the interaction of large substituent groups in both substrate and anion catalyst. The effect of bromine substitution in increasing the reaction velocity is shown to decrease as the reactivity of the ketone increases, and this is explained in terms of the charge distribution in the anion of the substrate.


2015 ◽  
Vol 108 (2) ◽  
pp. 550a
Author(s):  
John Weirich ◽  
Brianna Haight ◽  
Olivier Lequin ◽  
Lucie Khemtémourian ◽  
Ludovic Carlier ◽  
...  

2015 ◽  
Vol 31 (7) ◽  
pp. 1365-1373
Author(s):  
WANG Ji-Qian ◽  
◽  
SUN Ying-Jie ◽  
DAI Jing-Ru ◽  
ZHAO Yu-Rong ◽  
...  

Author(s):  
M.В. Кнатько ◽  
М.Н. Лапушкин

AbstractWe have studied transient processes of the thermal ionization of sodium on the surface of NaAu_ y semiconductor film under the action of a variable external electric field. It is established that the kinetics of Na^+ ion current during variation of the external field is determined by the establishment of charge distribution in the NaAu_ y film, while the efficiency of thermal ionization of Na atoms is related to the concentration of holes near the NaAu_ y /vacuum interface.


2020 ◽  
Vol 117 (5) ◽  
pp. 2456-2461 ◽  
Author(s):  
Robert Shelansky ◽  
Hinrich Boeger

Specificity in transcriptional regulation is imparted by transcriptional activators that bind to specific DNA sequences from which they stimulate transcription. Specificity may be increased by slowing down the kinetics of regulation: by increasing the energy for dissociation of the activator–DNA complex or decreasing activator concentration. In general, higher dissociation energies imply longer DNA dwell times of the activator; the activator-bound gene may not readily turn off again. Lower activator concentrations entail longer pauses between binding events; the activator-unbound gene is not easily turned on again and activated transcription occurs in stochastic bursts. We show that kinetic proofreading of activator–DNA recognition—insertion of an energy-dissipating delay step into the activation pathway for transcription—reconciles high specificity of transcriptional regulation with fast regulatory kinetics. We show that kinetic proofreading results from the stochastic removal and reformation of promoter nucleosomes, at a distance from equilibrium.


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