Accurate random coil chemical shifts from an analysis of loop regions in native states of proteins.
We present a method for calculating accurate random coil chemical shift values of proteins. These values are obtained by analyzing the relationship between the amino acid sequences in flexible loop regions of native states and the corresponding experimentally measured chemical shifts. We estimate the errors in the random coil chemical shift scales to be 0.31 ppm for (13)C(alpha), 0.37 ppm for (13)C(beta), 0.31 ppm for (13)CO, 0.68 ppm for (15)N, 0.09 ppm for (1)H, and 0.04 ppm for (1)H(alpha).
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Alfonso
A
De Simone
Andrea
A
Cavalli
Shang-Te Danny
ST
Hsu
Wim
W
Vranken
Michele
M
Vendruscolo
D000595:Amino Acid Sequence; D030562:Databases, Protein; D009682:Magnetic Resonance Spectroscopy / Q000379:methods* / Q000592:standards; D011487:Protein Conformation; D011506:Proteins / Q000032:analysis*; D012015:Reference Standards
D011506:Proteins