The thermal hydrogen/deuterium exchange behaviors of GlyProH(+), ProGlyH(+)
, and ValGlyH(+) in the reactions with D2O have been studied in a Fourier t
ransform ion cyclotron resonance mass spectrometer. The analyzed behaviors
are consistent with our earlier conclusions that more basic N-terninal amin
o acids lower the overall efficiency of the hydrogen atom exchange in proto
nated alkyl dipeptides, It appears that the mobility of a proton over the b
asic sites in peptides can be restricted drastically by N-terminal proline,
relative to peptides with other N-terminal alkyl amino acids. (C) 2000 Els
evier Science B.V.