Nano-ESI MS studies enable characterization of relative dimer stabilities of TIM mutants.

Mutations at positions 64 and 75 destabilize the dimeric structure.

The order of gas-phase stabilities is Wild Type > T75S > Q64E ∼ Q64N

Enzymatic activity of Q64N/E mutants is inhibited by a synthetic dimer interface peptide.

Inhibitory effects of an interface peptide on enzyme activity was more in case of Q64 mutants.