A multiple regression analysis has established a nonlinear relationship between the backbone dihedral angles and the C a coordinates obtained from the x-ray crystal structures of 14 proteins. The regression equations have been applied to predict specific dihedral angles of each residue in the backbo
Assigning secondary structure from protein coordinate data
β Scribed by Sonya M. King; W. Curtis Johnson
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 83 KB
- Volume
- 35
- Category
- Article
- ISSN
- 0887-3585
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β¦ Synopsis
We have developed a program to convert the three dimensional coordinates describing protein structure in the Brookhaven Data Bank into an assignment of secondary structure. The program assigns secondary structure in the same way a person assigns structure visually. It uses two angles and three distances to assign β£-helix, 3 10helix, β€-strand, hydrogen-bonded β€-turn, non-hydrogen-bonded β€-turn, and poly (L-proline) II type 3 1helix. The program is concerned with amide-amide interactions and should be particularly useful to spectroscopists. Proteins 1999;35:313-320.
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This article presents SOMCD, an improved method for the evaluation of protein secondary structure from circular dichroism spectra, based on Kohonen's self-organizing maps (SOM). Protein circular dichroism (CD) spectra are used to train a SOM, which arranges the spectra on a two-dimensional map. Loca
## Abstract Circular dichroism (CD) spectroscopy has been a valuable method for the analysis of protein secondary structures for many years. With the advent of synchrotron radiation circular dichroism (SRCD) and improvements in instrumentation for conventional CD, lower wavelength data are obtainab
The estimation of protein secondary structure from circular dichroism spectra is described by a multivariate linear model with noise (Gauss-Markoff model). With this formalism the adequacy of the linear model is investigated, paying special attention to the estimation of the error in the secondary s
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