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Crowding interactions perturb structure and stability by destabilizing the stable core of the α‐subunit of tryptophan synthase
Author(s) -
Kadumuri Rajashekar Varma,
Gullipalli Jagadeesh,
Subramanian SriVidya,
Jaipuria Garima,
Atreya Hanudatta S.,
Vadrevu Ramakrishna
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12259
Subject(s) - cooperativity , tryptophan synthase , tryptophan , ficoll , protein subunit , circular dichroism , denaturation (fissile materials) , chemistry , native state , biophysics , allosteric regulation , protein structure , macromolecular crowding , crystallography , protein secondary structure , biochemistry , biology , enzyme , amino acid , peripheral blood mononuclear cell , nuclear chemistry , macromolecule , in vitro , gene
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 (α 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 α 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.