The self association equilibrium of copper(II) hexanoate

1971 ◽  
Vol 24 (1) ◽  
pp. 187 ◽  
Author(s):  
PJ Burchill ◽  
JA McRae
Keyword(s):  
The Self ◽  
Self Association ◽  
Association Equilibrium

scholarly journals Solution Properties of Phycocyanin. IV. Studies of the Self-association Equilibrium of Phycocyanin in a pH 6.8 Solution

1977 ◽  
Vol 50 (11) ◽  
pp. 2892-2895 ◽  
Author(s):  
Naomichi Iso ◽  
Haruo Mizuno ◽  
Takahide Saito ◽  
Noriko Nitta ◽  
Katsuaki Yoshizaki
Keyword(s):  
The Self ◽  
Solution Properties ◽  
Self Association ◽  
Association Equilibrium

Determination of the self-association and inter-association equilibrium constants of a carboxylic acid and its mixtures with pyridine derivates

2006 ◽  
Vol 41 (1) ◽  
pp. 21-27 ◽  
Author(s):  
A. González ◽  
L. Irusta ◽  
M.J. Fernández-Berridi ◽  
J.J. Iruin ◽  
T. Sierra ◽  
...  
Keyword(s):  
Carboxylic Acid ◽  
Equilibrium Constants ◽  
The Self ◽  
Self Association ◽  
Association Equilibrium

Monte Carlo Study of the Self-association of Methanol in Benzene

1991 ◽  
Vol 6 (4-6) ◽  
pp. 299-310 ◽  
Author(s):  
Y. Adachi ◽  
K. Nakanishi
Keyword(s):  
Monte Carlo ◽  
Monte Carlo Study ◽  
The Self ◽  
Self Association

scholarly journals The C Terminus of the Ribosomal-Associated Protein LrtA is an Intrinsically Disordered Oligomer

2018 ◽  
Vol 19 (12) ◽  
pp. 3902 ◽  
Author(s):  
José L. Neira ◽  
A. Marcela Giudici ◽  
Felipe Hornos ◽  
Arantxa Arbe ◽  
Bruno Rizzuti
Keyword(s):  
Computational Modelling ◽  
Terminal Region ◽  
Physiological Conditions ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
C Terminus ◽  
Conformational Preferences ◽  
Self Association ◽  
Association Equilibrium ◽  
Post Stress

The 191-residue-long LrtA protein of Synechocystis sp. PCC 6803 is involved in post-stress survival and in stabilizing 70S ribosomal particles. It belongs to the hibernating promoting factor (HPF) family, intervening in protein synthesis. The protein consists of two domains: The N-terminal region (N-LrtA, residues 1101), which is common to all the members of the HPF, and seems to be well-folded; and the C-terminal region (C-LrtA, residues 102-191), which is hypothesized to be disordered. In this work, we studied the conformational preferences of isolated C-LrtA in solution. The protein was disordered, as shown by computational modelling, 1D-1H NMR, steady-state far- UV circular dichroism (CD) and chemical and thermal denaturations followed by fluorescence and far-UV CD. Moreover, at physiological conditions, as indicated by several biochemical and hydrodynamic techniques, isolated C-LrtA intervened in a self-association equilibrium, involving several oligomerization reactions. Thus, C-LrtA was an oligomeric disordered protein.

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