scholarly journals Cavity enhanced liquid-phase stopped-flow kinetics

The Analyst ◽  
2018 ◽  
Vol 143 (2) ◽  
pp. 493-502 ◽  
Author(s):  
Zuzana Bajuszova ◽  
Hanan Naif ◽  
Zulfiqur Ali ◽  
Joseph McGinnis ◽  
Meez Islam

The first application of cavity enhanced spectroscopy to liquid-phase stopped-flow kinetics.

1998 ◽  
Vol 63 (9) ◽  
pp. 3023-3031 ◽  
Author(s):  
Andrew G. Hadd ◽  
Alex L. Robinson ◽  
Kathy L. Rowlen ◽  
John W. Birks

Biochemistry ◽  
2010 ◽  
Vol 49 (24) ◽  
pp. 5066-5073 ◽  
Author(s):  
Robert S. Phillips ◽  
Santiago Lima ◽  
Roman Khristoforov ◽  
Bakthavatsalam Sudararaju

1987 ◽  
Vol 243 (1) ◽  
pp. 79-86 ◽  
Author(s):  
S R Patanjali ◽  
M J Swamy ◽  
A Surolia

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.


Biochemistry ◽  
1984 ◽  
Vol 23 (9) ◽  
pp. 2049-2056 ◽  
Author(s):  
Finn B. Hansen ◽  
Robert W. Noble ◽  
Murray J. Ettinger

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