scholarly journals Charge-Transfer Transitions in the Vacuum-Ultraviolet of Protein Circular Dichroism Spectra

2008 ◽  
Vol 112 (6) ◽  
pp. 1866-1874 ◽  
Author(s):  
Benjamin M. Bulheller ◽  
Andrew J. Miles ◽  
B. A. Wallace ◽  
Jonathan D. Hirst
Keyword(s):  
Circular Dichroism ◽  
Charge Transfer ◽  
Vacuum Ultraviolet ◽  
Circular Dichroism Spectra ◽  
Charge Transfer Transitions ◽  
Circular Dichroïsm

scholarly journals Synchrotron radiation circular dichroism and conventional circular dichroism spectroscopy: A comparison

2002 ◽  
Vol 16 (3-4) ◽  
pp. 121-125 ◽  
Author(s):  
J. G. Lees ◽  
B. A. Wallace
Keyword(s):  
Circular Dichroism ◽  
Charge Transfer ◽  
Synchrotron Radiation ◽  
Vacuum Ultraviolet ◽  
Light Sources ◽  
Extra Information ◽  
Charge Transfer Transitions ◽  
Conventional Instrument ◽  
First Time ◽  
Circular Dichroïsm

Conventional circular dichroism (cCD) spectroscopy is a valuable tool for secondary structure analyses of proteins. In recent years, it has been possible to use synchrotrons as light sources for CD, with the technique being known as Synchrotron Radiation Circular Dichroism (SRCD). In this study, the spectra of two proteins, the primarily helical myoglobin and the primarily beta‒sheet concanavalin A, have been collected on both a cCD instrument and on the SRCD at the Daresbury synchrotron and their characteristics were compared. Over the wavelength regions where both instruments are capable of making measurements (from about 300 to 175 nm) the spectra are very similar, except at the low wavelength extreme of the cCD spectra. In this region, the spectra deviate somewhat, due to the limitations of the light source intensity in the conventional instrument. The SRCD spectra extend to much lower wavelengths (160 nm). This additional low wavelength vacuum ultraviolet (VUV) data contains a large amount of extra information, including, for the first time, a number of peaks consistent with previously predicted charge transfer transitions.

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