Measurement of hydrogen exchange at the tryptophan residues of a protein by stopped-flow and ultraviolet spectroscopy

1978 ◽  
Vol 100 (1) ◽  
pp. 272-276 ◽  
Author(s):  
Mamoru Nakanishi ◽  
Hitomi Nakamura ◽  
Akiko Y. Hirakawa ◽  
Masamichi Tsuboi ◽  
Toshihiko Nagamura ◽  
...  
Keyword(s):  
Hydrogen Exchange ◽  
Ultraviolet Spectroscopy ◽  
Stopped Flow ◽  
Tryptophan Residues

Stopped-flow ultraviolet spectroscopy for hydrogen-exchange studies of nucleic acids

FEBS Letters ◽  
1977 ◽  
Vol 81 (1) ◽  
pp. 61-64 ◽  
Author(s):  
M. Nakanishi ◽  
M. Tsuboi ◽  
Y. Saijo ◽  
T. Nagamura
Keyword(s):  
Nucleic Acids ◽  
Hydrogen Exchange ◽  
Ultraviolet Spectroscopy ◽  
Stopped Flow

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.

Hydrogen exchange of the tryptophan residues in bovine ?-lactalbumin studied by uv spectroscopy

Biopolymers ◽  
1988 ◽  
Vol 27 (4) ◽  
pp. 629-644 ◽  
Author(s):  
Yoshiaki Harushima ◽  
Kunihiro Kuwajima ◽  
Shintaro Sugai
Keyword(s):  
Hydrogen Exchange ◽  
Uv Spectroscopy ◽  
Tryptophan Residues ◽  
Bovine Lactalbumin
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