التفاصيل البيبلوغرافية
| العنوان: |
Crowding interactions perturb structure and stability by destabilizing the stable core of the α-subunit of tryptophan synthase. |
| المؤلفون: |
Kadumuri, Rajashekar Varma1, Gullipalli, Jagadeesh1, Subramanian, SriVidya1, Jaipuria, Garima2, Atreya, Hanudatta S.2, Vadrevu, Ramakrishna1 |
| المصدر: |
FEBS Letters. Jul2016, Vol. 590 Issue 14, p2096-2105. 10p. |
| مصطلحات موضوعية: |
*TRYPTOPHAN synthase, *FICOLL, *CIRCULAR dichroism, *FLUORESCENCE spectroscopy, *DENATURATION of proteins, *NUCLEAR magnetic resonance |
| مستخلص: |
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. [ABSTRACT FROM AUTHOR] |
| قاعدة البيانات: |
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