Index of content:
Volume 111, Issue 6, 08 August 1999
Comment on “Improving protein circular dichroism calculations in the far-ultraviolet through reparametrizing the amide chromophore” [J. Chem. Phys. 109, 782 (1998)]111(1999); http://dx.doi.org/10.1063/1.479562View Description Hide Description
Circular dichroismspectra for 23 proteins have been calculated using transition parameters from experiments on model amides and semiempirical molecular orbital (MO) calculations. The results are substantially better than those reported by Hirst. The improvements result primarily from using distributed dipoles (monopoles), rather than the point dipoles used by Hirst.
Response to “Comment on ‘Improving protein circular dichroism calculations in the far-ultraviolet through reparameterizing the amide chromophore’ ” [J. Chem. Phys. 111, 2844 (1999)]111(1999); http://dx.doi.org/10.1063/1.479563View Description Hide Description
In response to Woody and Sreerama’s Comment that they have realized significant improvements in calculations of the circular dichroism of proteins over those reported by Hirst previously, we report the simultaneous and independent achievement of comparably accurate calculations. Our calculations are based on parameters from ab initiowave functions, in contrast to the combination of experimental data and semiempiricalwave functions used by Woody and Sreerama.