Studies on interaction of oligopeptides with sodium dodecyl sulfate: Stopped-flow kinetics of chemical modification of tryptophan residues withN-bromosuccinimide

1987 ◽  
Vol 6 (5) ◽  
pp. 401-411 ◽  
Author(s):  
Takeyoshi Imamura ◽  
Katsutoshi Konishi
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Chemical Modification ◽  
Sodium Dodecyl ◽  
Stopped Flow ◽  
Tryptophan Residues ◽  
Dodecyl Sulfate ◽  
Stopped Flow Kinetics ◽  
Kinetics Of

Kinetics of alkaline hydrolysis of ethylp-nitrophenyl ethylphosphonate in the reverse micellar system: sodium dodecyl sulfate-hexanol-water

2000 ◽  
Vol 49 (2) ◽  
pp. 265-269
Author(s):  
L. Ya. Zakharova ◽  
F. G. Valeeva ◽  
L. A. Kudryavtseva ◽  
V. E. Bel'skii ◽  
E. P. Zhil'tsova ◽  
...  
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Alkaline Hydrolysis ◽  
Sodium Dodecyl ◽  
Micellar System ◽  
Dodecyl Sulfate ◽  
Reverse Micellar System ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
System Sodium ◽  
Reverse Micellar

Influence of sodium dodecyl sulfate micelles on the kinetics of complex formation between Pd(H2O)42+ and glutathione

Polyhedron ◽  
1997 ◽  
Vol 16 (7) ◽  
pp. 1157-1160 ◽  
Author(s):  
Mihajilo S. Tošić ◽  
Vesna M. Vasić ◽  
Jovan M. Nedeljković ◽  
Ljubomir A. Ilić
Keyword(s):  
Complex Formation ◽  
Sodium Dodecyl Sulfate ◽  
Sodium Dodecyl ◽  
Dodecyl Sulfate ◽  
Kinetics Of

scholarly journals Studies on tryptophan residues of Abrus agglutinin. Stopped-flow kinetics of modification and fluorescence-quenching studies

1987 ◽  
Vol 243 (1) ◽  
pp. 79-86 ◽  
Author(s):  
S R Patanjali ◽  
M J Swamy ◽  
A Surolia
Keyword(s):  
Amino Acid ◽  
Protein A ◽  
Stopped Flow ◽  
Amino Acid Residues ◽  
Acidic Amino Acid ◽  
Native Protein ◽  
Tryptophan Residues ◽  
Stopped Flow Kinetics ◽  
Two Phases ◽  
Kinetics Of

The presence of two essential tryptophan residues/molecule was implicated in the binding site of Abrus agglutinin [Patanjali, Swamy, Anantharam, Khan & Surolia (1984) Biochem. J. 217, 773-781]. A detailed study of the stopped-flow kinetics of the oxidation of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues into two phases was observed upon ligand binding. The heterogeneity of tryptophan exposure was substantiated by quenching studies with acrylamide, succinimide and Cs+. Our study revealed the microenvironment of tryptophan residues to be hydrophobic, and also the presence of acidic amino acid residues in the vicinity of surface-localized tryptophan residues.

Isothermal Crystallization Kinetics of Sodium Dodecyl Sulfate–Water Micellar Solutions

2016 ◽  
Vol 16 (6) ◽  
pp. 3379-3388 ◽  
Author(s):  
Ruhina M. Miller ◽  
Andreas S. Poulos ◽  
Eric S. J. Robles ◽  
Nicholas J. Brooks ◽  
Oscar Ces ◽  
...  
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Crystallization Kinetics ◽  
Isothermal Crystallization ◽  
Sodium Dodecyl ◽  
Micellar Solutions ◽  
Isothermal Crystallization Kinetics ◽  
Dodecyl Sulfate ◽  
Kinetics Of
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