Determination of the secondary structure of proteins from the amide I band of the laser Raman spectrum

1981 ◽  
Vol 152 (4) ◽  
pp. 783-813 ◽  
Author(s):  
Robert W. Williams ◽  
A.Keith Dunker
Biopolymers ◽  
2008 ◽  
Vol 89 (11) ◽  
pp. 895-905 ◽  
Author(s):  
Yeqiu Wang ◽  
Reinhard I. Boysen ◽  
Bayden R. Wood ◽  
Mustafa Kansiz ◽  
Don McNaughton ◽  
...  

1979 ◽  
Author(s):  
J Marx ◽  
G Hudry-Clergeon ◽  
L Bernard

Raman spectroscopy is now a useful mean of estimating the secondary structure of proteins. The study of the Amide I and Amide III bands revealed an important increase in the β-sheet form of fibrin, compared with that of fibrinogen. This effect is accompanied by significant variations in the bands characteristic of aromatic chromophores. These observations favour the hypothesis (Hudry-Clergeon et al. 1975, Thromb. Res. 6, 533) that important structural events occur during the fibrinogenfibrin transition.


1979 ◽  
Author(s):  
J. Marx ◽  
G. Hudry-Clergeon ◽  
L. Bernard

Raman spectroscopy is now a useful mean of estimating the secondary structure of proteins. The study of the Amide I and Amide III bands revealed an important increase in the β-sheet form of fibrin, compared with that of fibrinogen. This effect is accompanied by significant variations in the bands characteristic of aromatic chromophores. These observations favour the hypothesis (Hudry-Clergeon et al.1975, Thromb. Res. 6, 533) that important structural events occur during the fibrinogenfibrin transition.


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