Figure 1 | Scientific Reports

Figure 1

From: Nucleotide-induced conformational changes of tetradecameric GroEL mapped by H/D exchange monitored by FT-ICR mass spectrometry

Figure 1

H/D exchange results for three GroEL domains.

The structural elements are identified above the sequence with 3 domains colored as in the top left GroEL monomer x-ray crystal structure, with line format designating helix/beta strand/random coil. For each of the proteolytic peptides common to apo GroEL and GroEL-ATPγS, the relative D-uptake difference (ARDD, liganded minus apo, averaged over all HDX incubation periods, ti) is calculated as shown in the bottom left equation. The results from all peptides are combined such that short peptides are mapped below the sequence and longer peptides are then chosen to fill any gaps. Color coding for ARDD values is shown at bottom right.

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