  The changes in the local and global dynamics of azide-labelled Lysozyme
compared with that of the wild type protein are quantitatively assessed for all
alanine residues along the polypeptide chain. Although attaching -N$_3$ to
alanine residues has been considered to be a minimally invasive change in the
protein it is found that depending on the location of the Alanine residue the
local and global changes in the dynamics differ. For Ala92 the change in the
cross correlated motions are minimal whereas attaching -N$_3$ to Ala90 leads to
pronounced differences in the local and global correlations as quantified by
cross correlation coefficients of the C$_{\alpha}$ atoms. It is also
demonstrated that the spectral region of the asymmetric azide stretch
distinguishes between alanine attachment sites whereas changes in the low
frequency, far-infrared region are less characteristic.
