The Effects of Biological Environments on the Electron-Relay Functionality of Tryptophan Residues in Proteins

ChemPhysChem ◽  
2011 ◽  
Vol 13 (1) ◽  
pp. 183-192 ◽  
Author(s):  
Xiaohua Chen ◽  
Hongjing Dai ◽  
Jilai Li ◽  
Xuri Huang ◽  
Zidong Wei
Keyword(s):  
Tryptophan Residues

The rates of photodestruction of tryptophan residues in human and bovine ocular lens proteins

1981 ◽  
Vol 32 (6) ◽  
pp. 747-754 ◽  
Author(s):  
R.F Borkman ◽  
J.D Tassin ◽  
S Lerman
Keyword(s):  
Ocular Lens ◽  
Lens Proteins ◽  
Tryptophan Residues

scholarly journals Role of Tryptophan Residues in Gramicidin Channel Organization and Function

2008 ◽  
Vol 95 (1) ◽  
pp. 166-175 ◽  
Author(s):  
Amitabha Chattopadhyay ◽  
Satinder S. Rawat ◽  
Denise V. Greathouse ◽  
Devaki A. Kelkar ◽  
Roger E. Koeppe
Keyword(s):  
Gramicidin Channel ◽  
Tryptophan Residues ◽  
And Function

The interaction of bovine milk caseins with the detergent sodium dodecyl sulphate. II. The effect of detergent binding on spectral properties of caseins

1970 ◽  
Vol 37 (2) ◽  
pp. 259-267 ◽  
Author(s):  
G. C. Cheeseman ◽  
Dorothy J. Knight
Keyword(s):  
Sodium Dodecyl Sulphate ◽  
Sodium Dodecyl ◽  
Bovine Milk ◽  
Difference Spectrum ◽  
Temperature Dependent ◽  
Difference Spectra ◽  
Negative Change ◽  
Tryptophan Residues ◽  
Hydrophobic Binding ◽  
The Difference

SummaryThe dissociation of casein aggregates by the detergent sodium dodecyl sulphate (SDS) gave rise to difference spectra and these spectra were characteristic for each of the different types of casein. Increase in absorption by the chromophore groups, tyrosine and tryptophan, when αs1- and β-casein aggregates were dissociated indicated binding of the detergent at regions of the molecule containing these residues. A decrease in absorption when κ-casein was dissociated indicated that the tyrosine and tryptophan residues were not in the region of the molecule to which the detergent was bound and that in the κ-casein aggregate these residues were in a more hydrophobic environment. Peaks on the difference spectra were obtained at 280 and 288 nm for αs1-casein and 284 and 291 nm for β-casein and troughs at 278 and 286 nm for κ-casein. The difference spectrum reached a maximum value when the αsl- and β-casein aggregates were dissociated and the further binding of SDS did not alter this value. The large negative change in the difference spectrum of κ-casein did not occur until after most of the aggregates were dissociated and did not reach a maximum until binding with SDS was complete. The value obtained for ΔOD was found to be temperature-dependent for β-casein-SDS interaction, but not for αs1- and κ-casein. Changes in spectra were also observed when αs1- and κ-casein interacted to form aggregates. The data obtained confirmed the importance of hydrophobic binding in casein aggregate formation and indicated the possible involvement of tyrosine and tryptophan residues in this binding.

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