Secondary Structure of Proteins Through Circular Dichroism Spectroscopy

1988 ◽  
Vol 17 (1) ◽  
pp. 145-166 ◽  
Author(s):  
W C Johnson
1973 ◽  
Vol 28 (3-4) ◽  
pp. 128-130 ◽  
Author(s):  
Wilhelm Menke ◽  
Rolf-Dieter Hirtz

With reference spectra derived from proteins of known structure (CHEN, YANG, and MARTINEZ, Biochemistry 11, 4120 [1972]) a better approximation of the circular dichroism spectrum of fragments of the thylakoid membrane is achieved, than by the use of polylysine as reference substance. Most probably the protein in the thylakoid membrane consists of 40 per cent helix, 42 per cent random coil and 18 per cent β-structure.


1988 ◽  
Vol 4 (4) ◽  
pp. 479-482 ◽  
Author(s):  
Luis Menéndez-Arias ◽  
Julián Gómez-Gutiérrez ◽  
Miguel García-Ferrández ◽  
Alvaro García-Tejedor ◽  
Federico Morán

2021 ◽  
Vol 43 (2) ◽  
pp. 58-64
Author(s):  
Alison Rodger ◽  
Doug Marshall

Circular dichroism (CD) is used to give information about the chirality or handedness of molecular systems. It is particularly widely applied to determine the secondary structure of proteins such as biopharmaceutical products.


1977 ◽  
Vol 55 (24) ◽  
pp. 4257-4266 ◽  
Author(s):  
Lewis A. Slotin ◽  
Denis R. Lauren ◽  
Ross E. Williams

Several polypeptides have been synthesized which contain the alternating sequence lysyl-X, where X = gly, L-ala, D-ala, L-val, L-leu, and L-phe. The polypeptides have been characterized by gel filtration (molecular weight) and by circular dichroism spectroscopy (secondary structure).


2013 ◽  
Vol 104 (2) ◽  
pp. 567a
Author(s):  
András Micsonai ◽  
Eszter Szabó ◽  
Wien Frank ◽  
Matthieu Réfrégiers ◽  
József Kardos

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