[A comparison of X-ray diffraction analysis and nuclear magnetic resonance from the data on the identification of alpha-helices and beta-strands in the same proteins].
The methods of X-ray diffraction analysis and nuclear magnetic resonance spectroscopy were compared using the data on the identification of alpha-helices and beta-strands of the same proteins. The goal of the study was to determine whether these identifications can be considered as equivalent in the structural classification of proteins and in the solution of other problems. The identifications obtained by the method of Kabsch and Sander for 56% specially chosen water-soluble proteins were chosen. It was found that the identification of alpha-helices and beta-strands are almost equivalent if used for the structural classification of the proteins. In the analysis of the conformational properties of amino acid residues or their combinations, it is reasonable to use the identifications of alpha-helices and beta-strands, obtained only from the data of X-ray diffraction analysis. An additional outcome of the study is a unique collection of pairs of protein structures obtained by the methods of X-ray diffraction analysis and nuclear magnetic resonance spectroscopy for the same proteins.
Shestopalov
B V
BV
D018360:Crystallography, X-Ray / Q000379:methods; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
D011506:Proteins