Fig 1.
Domain-swapped oligomers with different regions marked.
Fig 2.
Strategy used to study pH-dependent domain swapping process.
Fig 3.
A) Input for pH-dependent energy profile for DSI using (Swapped domain N-terminal alpha-helix in this case). B) Input for pH-dependent energy profile for NSI (Excluding swapped domain N-terminal alpha-helix in this case).
Table 1.
Amino acid propensity of DSI and NSI of pH dependent domain-swapped proteins with reference to non-redundant 3Dswapplus entries.
Table 2.
Relative thermal stability of DSI and NSI at D-pH and M-pH.
Fig 4.
Classical pH-dependent profile.
Fig 5.
Proposed model representing possible effects of pH on DSI(SI) and NSI (PI) during pH-dependent domain-swapping.
Fig 6.
pH-dependent energy profile of diphtheria toxin (1DDT).
Fig 7.
Interactions within domain swapped dimer of diphtheria toxin.
A) Three salt bridges within DSI. B) Unfavourable electrostatic interactions between negatively charged residues within NSI.
Fig 8.
pH-dependent energy profile of prion dimer (3HAF).
Fig 9.
Interactions within domain swapped dimer of prion protein.
A) Several strong and weak favourable ionic interactions between charged residues at DSI(shown in blue dotted lines). B) Several positively charged residues at NSI (shown in red color).
Fig 10.
Distribution of difference between binding energies at pH 7 and 3.
A) For DSI in 3Dswapplus entries. B) For DSI in 3DSwapplus entries and protein-protein interface in transient complexes
Fig 11.
Distribution of difference between dimerization pH (D-pH) and pI in general homodimers.
Table 3.
pI, D-pH and M-pH values for pH-dependent domain-swapped proteins.