Analysis of subsecond protein dynamics by amide hydrogen exchange and mass spectrometry using a quenched-flow setup
Protein Sci Rist et al.
14: 626
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Supplementary Figure 1: Quenched-flow amide hydrogen exchange of full-length apo-myoglobin. Protein mass spectra (left) and deconvoluted mass spectra (right) of apo-myoglobin after exposure to D2O for different times.
Supplementary Figure 2: Amide hydrogen exchange of peptide segments within the E. coli heat shock transcription factor sigma 32[superscript]. Regions of mass spectra showing five different peptic peptides of the E. coli heat schock transcritption factor sigma 32[superscript] after exposure to D2O for different times. The respective residue numbers of the peptides are indicated at the top.