Determination of the secondary structure of proteins by laser Raman spectroscopy

1976 ◽  
Vol 98 (22) ◽  
pp. 7075-7080 ◽  
Author(s):  
J. L. Lippert ◽  
D. Tyminski ◽  
P. J. Desmeules
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.


1976 ◽  
Vol 29 (3) ◽  
pp. 507 ◽  
Author(s):  
RP Cooney ◽  
NT Tam

Changes in the Raman spectrum of pyridine on a silica surface with increasing surface coverage may be used to determine the monolayer capacity. The method, which is independent of the BET method, produces a result which is in quantitative agreement with the BET result.


Biopolymers ◽  
2008 ◽  
Vol 89 (11) ◽  
pp. 895-905 ◽  
Author(s):  
Yeqiu Wang ◽  
Reinhard I. Boysen ◽  
Bayden R. Wood ◽  
Mustafa Kansiz ◽  
Don McNaughton ◽  
...  

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