Fig. 5: HDX-MS reveals GAPDH binding sites on trigger factor and suggests that bound GAPDH is monomeric.
From: Trigger factor both holds and folds its client proteins

a Woods plot showing the summed difference in deuterium uptake in trigger factor over all measured time points, comparing trigger factor alone and trigger factor in the presence of GAPDH. Peptides coloured blue and red are protected and deprotected from exchange in the presence of GAPDH (see the “Methods” section). Peptides with no significant difference between conditions, determined using a 99% confidence interval (dotted line), are shown in grey. b The differences in deuterium uptake plotted on the structure of trigger factor (PDB: 1J0X). Blue and red regions are protected or deprotected from exchange, respectively, in the presence of GAPDH. c Woods plot showing the summed difference in deuterium uptake over all measured time points (0.5, 2, 5, 10 and 30 min) between refolding GAPDH and GAPDH in complex with TF. Peptides coloured red are deprotected from exchange in the presence of GAPDH (see the “Methods” section). No peptides show statistically significant protection in the presence of GAPDH. Peptides with no significant difference between conditions, determined using a 99% confidence interval (dotted line), are shown in grey. d The differences in deuterium uptake plotted on the structure of GAPDH (right) PDB: 1J0X. Red regions are deprotected from exchange when bound to trigger factor.