Abstract
The distribution of chemical shifts in 1H nuclear magnetic resonance spectra of water-soluble, diamagnetic polypeptides and proteins has been analyzed on the basis of the available data from those polypeptides (proteins) where almost all resonances have been assigned by two-dimensional nuclear magnetic resonance methods. As to be expected from theory, the mean values of chemical shifts differ significantly from the known “random coil” values. The analysis of data leads to a description of the corresponding probability distributions permitting a more reliable use of chemical shifts for pattern recognition in two-dimensional spectra of proteins.
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