Mass spectrometric analysis of dimer-disrupting mutations in Plasmodium triosephosphate isomerase
详细信息 查看全文
- 作者：Debarati Bandyopadhyay ; Sunita Prakash ; Kallol Gupta1 ; Padmanabhan Balaram ; pb@mbu.iisc.ernet.in" class="auth_mail" title="E-mail the corresponding author
- 关键词：Triosephosphate isomerase ; Protein mass spectrometry ; Gas phase dimers ; Protein dimer stability ; Triosephosphate isomerase interface mutants
- 刊名：Analytical Biochemistry
- 出版年：2016
- 出版时间：1 May 2016
- 年：2016
- 卷：500
- 期：Complete
- 页码：45-50
- 全文大小：2379 K
文摘
- •
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.