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Crowding interactions perturb structure and stability by destabilizing the stable core of the alpha-subunit of tryptophan synthase

Kadumuri, Rajashekar Varma and Gullipalli, Jagadeesh and Subramanian, SriVidya and Jaipuria, Garima and Atreya, Hanudatta S and Vadrevu, Ramakrishna (2016) Crowding interactions perturb structure and stability by destabilizing the stable core of the alpha-subunit of tryptophan synthase. In: FEBS LETTERS, 590 (14). pp. 2096-2105.

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Official URL: http://dx.doi.org/10.1002/1873-3468.12259

Abstract

The consequences of crowding derived from relatively small and intrinsically disordered proteins are not clear yet. We report the effect of ficoll-70 on the structure and stability of native and partially folded states of the 29 kDa alpha subunit of tryptophan synthase (alpha TS). Overall, combining the changes in the circular dichroism and fluorescence spectra, in conjunction with the gradual loss of cooperativity under urea denaturation in the presence of increasing amounts of ficoll, it may be concluded that the crowding agent perturbs not only the native state but also the partially folded state of alpha TS. Importantly, NMR data indicate that ficoll interacts with the residues that constitute the stable core of the protein thus shedding light on the origin of the observed perturbation.

Item Type: Journal Article
Additional Information: Copy right for this article belongs to the WILEY-BLACKWELL, 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
Department/Centre: Division of Chemical Sciences > NMR Research Centre (Formerly Sophisticated Instruments Facility)
Depositing User: Id for Latest eprints
Date Deposited: 22 Oct 2016 06:51
Last Modified: 22 Oct 2016 06:51
URI: http://eprints.iisc.ac.in/id/eprint/54662

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