A new procedure based on the statistical method of "variable selection" is used to predict the secondary structure of proteins from circular dichroism spectra. Variable selection adds the flexibility found in the Provencher and GlΓΆckner method (S. W. Provencher and J. GlΓΆckner, 1981, Biochemistry 20
Effects of Relative Band Intensity on Prediction of Protein Secondary Structure from CD
β Scribed by A. Toumadje; W.C. Johnson
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 200 KB
- Volume
- 211
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
Increasing the magnitude of a protein CD spectrum obviously increases the magnitude of each predicted secondary structure by the same amount. However, increasing the magnitude of the negative, long-wave-length portion of a protein CD spectrum usually has the opposite effect from increasing the positive, short-wave-length portion. Thus small distortions in the CD spectra of proteins at short wavelength can have a significant effect on the analysis for secondary structure. This measurement error and its effect on the analysis are systematically investigated for 16 proteins of known structure. 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.
π SIMILAR VOLUMES
Fourier self-deconvolution (FSD) was performed on protein amide I and II Fourier transform infrared (FTIR) spectra to test if the resultant increased band shape variation would lead to improvements in protein secondary structure prediction with our factor analysis based restricted multiple regressio