scholarly journals Kinetic Study on Conformational Changes of Poly(L-lysine) in Sodium Alkyl Sulfate Solutions. Effects of Surfactant Chain Length and Added NaCl

1982 ◽  
Vol 55 (4) ◽  
pp. 985-989 ◽  
Author(s):  
Kunio Takeda ◽  
Akira Iba ◽  
Keishiro Shirahama
Keyword(s):  
Kinetic Study ◽  
Chain Length ◽  
Conformational Changes ◽  
Alkyl Sulfate ◽  
Sulfate Solutions

STABILITY OF COLLOIDAL ALUMINA DISPERSION IN AQUEOUS ALKYL SULFATE SOLUTIONS

2007 ◽  
Vol 14 (03) ◽  
pp. 395-401 ◽  
Author(s):  
SHAOXIAN SONG ◽  
YIMIN ZHANG
Keyword(s):  
Aqueous Solutions ◽  
Chain Length ◽  
Hydrocarbon Chain ◽  
Alkyl Sulfate ◽  
Experimental Results ◽  
Sulfate Concentration ◽  
Sulfate Solutions ◽  
Hydrocarbon Chain Length ◽  
Alkyl Sulfates

Coagulation of colloidal alumina in aqueous solutions in the absence or presence of alkyl sulfates has been studied by means of measurements of electrokinetics, adsorption, and coagulate size in this work. The experimental results showed that the coagulation of colloidal alumina in aqueous alkyl sulfate solutions was much stronger than that in aqueous electrolytic solutions. It closely correlated with particle hydrophobicity rendered by the adsorption of alkyl sulfate anions on alumina/water interfaces, indicating hydrophobic coagulation. Also, it has been found that the hydrocarbon chain length of alkyl sulfate strongly influences the hydrophobic coagulation. The longer the chain, the stronger the coagulation and the lower the alkyl sulfate concentration needed for achieving the maximum coagulation degree.

Influence of chain length on the sphere-to-rod transition in alkyl sulfate micelles

1983 ◽  
Vol 87 (7) ◽  
pp. 1264-1277 ◽  
Author(s):  
Paul J. Missel ◽  
Norman A. Mazer ◽  
George B. Benedek ◽  
Martin C. Carey
Keyword(s):  
Chain Length ◽  
Alkyl Sulfate

THE "FOLDING" BEHAVIORS OF HOMOPOLYMERS WITH ONE END FIXED

2004 ◽  
Vol 18 (15) ◽  
pp. 2123-2139 ◽  
Author(s):  
BIN XUE ◽  
JUN WANG ◽  
WEI WANG
Keyword(s):  
Molecular Dynamics ◽  
Chain Length ◽  
Conformational Changes ◽  
Canonical Ensemble ◽  
Interaction Strength ◽  
Simulation Method ◽  
Dynamics Simulation ◽  
Radius Of Gyration ◽  
Native Conformation ◽  
Collapse Temperature

We study the "folding" behaviors of homopolymers with one end fixed. By using canonical ensemble molecular dynamics simulation method, we observe the conformational changes during folding processes. Long chains collapse to the helical nuclei, then regroup to helix from the free-end to form the compact conformations through the middle stages of helix-like coil and helix-like cone, while short chains do not apparently have the above mentioned middle stages. Through simulated annealing, the native conformation of homopolymer chain in our model is found to be helix. We show the relations between specific heat C v (T) and radius of gyration R g (T) as functions of temperature, chain length and the interaction strength, respectively. We find that these two quantities match well and can be combined to interpret the "folding" process of the homopolymer. It is found that the collapse temperature Tθ and the native-like folding temperature T f do not change with the chain length in our model, however the interaction strength affects the values of Tθ and T f .

scholarly journals Conformational Changes and Possible Structure of the Oxoglutarate Translocator of Rat-Heart Mitochondria Revealed by the Kinetic Study of Malate and Oxoglutarate Uptake

1983 ◽  
Vol 134 (3) ◽  
pp. 397-405 ◽  
Author(s):  
Claudine M. SLUSE-GOFFART ◽  
Francis E. SLUSE ◽  
Claire DUYCKAERTS ◽  
Marc RICHARD ◽  
Paul HENGESCH ◽  
...  
Keyword(s):  
Kinetic Study ◽  
Conformational Changes ◽  
Rat Heart ◽  
Heart Mitochondria ◽  
Rat Heart Mitochondria

Effect of alcohol chain length on the enzymatic resolution of racemic mandelic acid and kinetic study

2014 ◽  
pp. n/a-n/a ◽  
Author(s):  
Yang Pan ◽  
Ke-Wen Tang ◽  
Chang-Qing He ◽  
Wei Yi ◽  
Wei Zhu ◽  
...  
Keyword(s):  
Kinetic Study ◽  
Chain Length ◽  
Mandelic Acid ◽  
Enzymatic Resolution

scholarly journals Activation of dihydrofolate reductase following thiol modification involves a conformational change at the active site

1998 ◽  
Vol 335 (3) ◽  
pp. 643-646 ◽  
Author(s):  
Ying-Xin FAN ◽  
Zhen-Yu LI ◽  
Li ZHU ◽  
Jun-Mei ZHOU
Keyword(s):  
Kinetic Study ◽  
Conformational Change ◽  
Dihydrofolate Reductase ◽  
Conformational Changes ◽  
Active Site ◽  
Chinese Hamster ◽  
Intrinsic Fluorescence ◽  
Activation Mechanism ◽  
Slow Phase ◽  
Ideal System

Compared with the activation of dihydrofolate reductase (DHFR) by protein denaturants and inorganic salts, activation of the enzyme by thiol modification is relatively slow. Thus it is an ideal system for kinetic study of the activation mechanism. We describe here a kinetic study of the activation of DHFRs from chicken liver and Chinese hamster ovary by p-hydroxymercuribenzoate (p-HMB). The conformational changes in the enzyme molecule that result from the modification were monitored by measuring fluorescence enhancement due to the binding of 2-p-toluidinylnaphthalene-6-sulphonate (TNS), and by monitoring changes in the intrinsic fluorescence of the enzyme. Both activation and the conformational change probed by TNS followed pseudo-first-order kinetics, and the rate constants obtained are in good agreement with each other. The change in intrinsic fluorescence is a biphasic process. The rate of the fast phase, which may reflect a change in the microenvironment of Trp-24 at the active site, coincides with the rate of activation and the conformational change probed by TNS. The rate of the slow phase, which reflects a global conformational change, is about one order of magnitude lower than that of activation. The results indicate that the activation of DHFR by p-HMB is due to modification-induced conformational changes at its active site, rather than the modification of the thiol group itself, which is almost complete within the dead-time of the experiment. This study provides kinetic evidence for the proposal that flexibility at the active site is essential for full expression of catalytic activity.

Partial molal volumes in alkyl sulfate solutions

1956 ◽  
Vol 11 (4-5) ◽  
pp. 352-355 ◽  
Author(s):  
Eric Hutchinson ◽  
Carol S. Mosher
Keyword(s):  
Alkyl Sulfate ◽  
Sulfate Solutions ◽  
Partial Molal Volumes ◽  
Molal Volumes
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