scholarly journals A new method for determining protein secondary structure by laser raman spectroscopy applied to FD phage

1980 ◽  
Vol 32 (1) ◽  
pp. 232-234 ◽  
Author(s):  
R.W. Williams ◽  
A.K. Dunker ◽  
W.L. Peticolas
Keyword(s):  
Raman Spectroscopy ◽  
Secondary Structure ◽  
Protein Secondary Structure ◽  
New Method ◽  
Laser Raman Spectroscopy ◽  
Laser Raman

Laser Raman Spectroscopy of Fibrinogen and Fibrin

1979 ◽  
Author(s):  
J Marx ◽  
G Hudry-Clergeon ◽  
L Bernard
Keyword(s):  
Raman Spectroscopy ◽  
Secondary Structure ◽  
Laser Raman Spectroscopy ◽  
Laser Raman ◽  
Secondary Structure Of Proteins ◽  
Β Sheet ◽  
Structure Of Proteins

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.

Phage .vphi.X174 probed by laser Raman spectroscopy: evidence for capsid-imposed constraint on DNA secondary structure

Biochemistry ◽  
1987 ◽  
Vol 26 (6) ◽  
pp. 1532-1538 ◽  
Author(s):  
N. L. Incardona ◽  
B. Prescott ◽  
D. Sargent ◽  
O. P. Lamba ◽  
G. J. Thomas
Keyword(s):  
Raman Spectroscopy ◽  
Secondary Structure ◽  
Laser Raman Spectroscopy ◽  
Dna Secondary Structure ◽  
Laser Raman

Laser Raman Spectroscopy of Fibrinogen and Fibrin

1979 ◽  
Author(s):  
J. Marx ◽  
G. Hudry-Clergeon ◽  
L. Bernard
Keyword(s):  
Raman Spectroscopy ◽  
Secondary Structure ◽  
Laser Raman Spectroscopy ◽  
Laser Raman ◽  
Secondary Structure Of Proteins ◽  
Β Sheet ◽  
Structure Of Proteins

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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