W. C. Johnson

TL;DR: Although the variable selection method improves the analysis of circular dichroism data truncated at 190 nm, data measured to 178 nm gives superior results, it is shown that improving the fit to the measured CD beyond the accuracy of the data can result in poorer analyses.

TL;DR: This paper shows how this method is based on the construction of the generalized inverse from the singular value decomposition of a set of CD spectra corresponding to proteins whose secondary structures are known from X-ray crystallography without resorting to least-squares fitting and standard matrix inversion techniques.

TL;DR: Seven types of error that may interfere with the analysis of protein circular dichroism (CD) spectra for secondary structure are examined and it is found that small errors in the baseline will rationalize poor analyses.

TL;DR: A method to correct the CD spectra of peptides undergoing the helix-coil transition for contributions due to absorbing side chains using singular value decomposition and the resulting coefficients from the fitting are used along with the common basis vectors to regenerate the entire corrected spectrum.

TL;DR: The results demonstrate that a two-point calibration of a CD instrument is mandatory to avoid serious errors when estimating secondary structure from protein CD spectra.