Extended Data Fig. 4: Mass spectrometry confirms coexistence of multiple species for KWOCAs 18 and 70.
From: Local structural flexibility drives oligomorphism in computationally designed protein assemblies
(a) Comparison between the (top) experimental and (bottom) simulated native mass spectra from Fig. 2f,g. A 0.5:1:1.25 ratio of 9.3-, 10-, and 12-trimer assemblies was used in the simulation for KWOCA 18, and a 1:1.25 ratio of 12- and 14-trimer assemblies for KWOCA 70. (b) Tandem mass spectra by higher-energy collisional dissociation (HCD) with isolation m/z ranges of (left) 12,500-13,500 and (right) 14,500-15,500 for KWOCA 18, and isolation m/z ranges of (left) 15,000–16,000 and (right) 16,500–17,500 for KWOCA 70. (c) Conventional native mass spectra with lower m/z ranging from 4,500–10,000 and 4,000–14,500 for KWOCAs 18 and 70, respectively. The inset shows both 2D and 1D spectra of the deconvoluted masses from co-occurring low mass species.
