The chiroptical properties of proteins. II. Near-ultraviolet circular dichroism of lysozyme

Biopolymers ◽  
1980 ◽  
Vol 19 (12) ◽  
pp. 2191-2208 ◽  
Author(s):  
Warren J. Goux ◽  
Thomas M. Hooker
Keyword(s):  
Circular Dichroism ◽  
Chiroptical Properties ◽  
Near Ultraviolet ◽  
Circular Dichroïsm

The near infra red (NIR) chiroptical properties of nickel dithiolene complexes

2015 ◽  
Vol 39 (1) ◽  
pp. 122-129 ◽  
Author(s):  
Yann Le Gal ◽  
Antoine Vacher ◽  
Vincent Dorcet ◽  
Marc Fourmigué ◽  
Jeanne Crassous ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Thin Layer ◽  
Chiroptical Properties ◽  
Infra Red ◽  
Redox Switching ◽  
Circular Dichroïsm

Circular dichroism (CD) thin layer spectro-electrochemical experiments reveal a redox switching of CD-active bands in the NIR region.

Characterization of a ribonuclease S refolding intermediate

1993 ◽  
Vol 345 (1674) ◽  
pp. 131-140
Keyword(s):  
Circular Dichroism ◽  
Cd Spectrum ◽  
Near Ultraviolet ◽  
Circular Dichroïsm

D uring ribonuclease S (RN ase S) refolding, two peptide fragm ents recognize each other, and bind to g eth er to form a refolding in term ediate which slowly converts to th e nativ e state. We have characterized this refolding interm ediate using absorbance, circular dichroism (CD), and nuclear m agnetic resonance (NMR) spectroscopies. These techniques reveal significant am ounts of bo th secondary and te rtia ry stru ctu re ; the in term ediate differs from a m olten globule in being packed and native-like, b u t it resembles a m olten globule in having no near-ultraviolet (UV) CD spectrum . Final refolding is slow and accom panies proline isom erization. The results show th a t a t least two separate stages are observed in the form ation of the te rtia ry stru ctu re of RNaseS.

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