Fig. 1: Quantifying the relationship between modification change and proximity to interface.
From: Protein complex prediction using Rosetta, AlphaFold, and mass spectrometry covalent labeling
a Breakdown of the residues with a modification change of at least 40%, within and outside the binding interfaces of a specified complex. The residues shown in Panel (a) are a subset of the residues shown in Panel c. b Visualization of the four labeled residues with large modification changes (see Panel a) for one subunit of the β−2-microglobulin homodimer crystal structure. The labeled residues are colored in blue, the respective closest residue on a different subunit of the complex is colored in green, and the interface distance between them is shown above the dotted yellow line. c Linear correlation between modification changes of all labeled residues and the interface distances, where larger modification changes are expected for residues at the interface (x = 0). Source data are provided as a Source Data file.
