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Mass spectrometric analysis of dimer-disrupting mutations in Plasmodium triosephosphate isomerase

Bandyopadhyay, Debarati and Prakash, Sunita and Gupta, Kallol and Balaram, Padmanabhan (2016) Mass spectrometric analysis of dimer-disrupting mutations in Plasmodium triosephosphate isomerase. In: ANALYTICAL BIOCHEMISTRY, 500 . pp. 45-50.

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Official URL: http://dx.doi.org/10.1016/j.ab.2016.02.011


Electrospray ionization mass spectrometry (ESI MS) under nanospray conditions has been used to examine the effects of mutation at two key dimer interface residues, Gln (Q) 64 and Thr (T) 75, in Plasmodium falciparum triosephosphate isomerase. Both residues participate in an intricate network of intra- and intersubunit hydrogen bonds. The gas phase distributions of dimeric and monomeric protein species have been examined for the wild type enzyme (TWT) and three mutants, Q64N, Q64E, and 175S, under a wide range of collision energies (40-160 eV). The results established the order of dimer stability as TWT > T75S > Q64E similar to Q64N. The mutational effects on dimer stability are in good agreement with the previously reported estimates, based on the concentration dependence of enzyme activity. Additional experiments in solution, using inhibition of activity by a synthetic dimer interface peptide, further support the broad agreement between gas phase and solution studies. (C) 2016 Elsevier Inc. All rights reserved.

Item Type: Journal Article
Additional Information: Copy right for this article belongs to the ACADEMIC PRESS INC ELSEVIER SCIENCE, 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA
Keywords: Triosephosphate isomerase; Protein mass spectrometry; Gas phase dimers; Protein dimer stability; Triosephosphate isomerase interface mutants
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 11 May 2016 07:54
Last Modified: 11 May 2016 07:54
URI: http://eprints.iisc.ac.in/id/eprint/53804

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