Abstract
A new approach is presented to estimate secondary structures in globular proteins in solution from vacuum ultraviolet circular dichroism.Two new important Improvements are introduced compared to previous methods. Circular dichroism measurements are extended to vacuum ultraviolet down to 165 nm, the limit imposed by water transmittance. The second improvement concerns the contribution of reverse turns (β-turns) to the secondary structure and the addition of new reference spectra.Estimates of secondary structures from analyses of circular dichroism spectra in solution of the different classes of proteins are in close agreement with X-ray diffraction of the crystals. However for Rubredoxin, a small molecular weight protein (6000 Daltons), a conformational change in secondary structure is found to occur in going from cristalline state to aqueous solution.
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