Circular dichroism studies of angiotensin II and analogs: effects of primary sequence, solvent, and pH on the side-chain conformation

Biochemistry ◽  
1977 ◽  
Vol 16 (4) ◽  
pp. 806-812 ◽  
Author(s):  
Karl Lintner ◽  
Serge Fermandjian ◽  
Pierre Fromageot ◽  
Mahesh C. Khosla ◽  
Robert R. Smeby ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Angiotensin Ii ◽  
Chain Conformation ◽  
Side Chain ◽  
Primary Sequence ◽  
Side Chain Conformation ◽  
Circular Dichroïsm

Circular Dichroism, Self Interaction and Side Chain Conformation of Riboflavin and Riboflavin Analogues

1972 ◽  
Vol 27 (9) ◽  
pp. 1044-1046 ◽  
Author(s):  
G. Scola-Nagelschneider ◽  
P. Hemmerich
Keyword(s):  
Circular Dichroism ◽  
Ionic Strength ◽  
Aqueous Solutions ◽  
Chain Conformation ◽  
Side Chain ◽  
Cd Spectra ◽  
Polar Solvents ◽  
Side Chain Conformation ◽  
Vibronic Transitions ◽  
Circular Dichroïsm

The CD-spectra of riboflavin and riboflavin analogues in aqueous solutions differ very little depending on pH and ionic strength, but are extremely sensitive upon solvent changes. The two bands in the region of 300 —500 nm seen in aqueous solutions are split into seven bands in less polar solvents, which can be assigned to seven vibronic transitions. The spectra may be interpreted by “through space” and “through chain” interactions of the sidechain centers of chirality with the flavin chromophore, which influence the two first π —π* transitions in different manner.

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