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An obligatory intermediate controls the folding of the alpha-subunit of tryptophan synthase, a TIM barrel protein

Wintrode, P.L.; Rojsajjakul, T.; Vadrevu, R.; Matthews, C.Robert.; Smith, D.L.

Journal of Molecular Biology 347(5): 911-919

2005

ISSN/ISBN: 0022-2836
PMID: 15784252
DOI: 10.1016/j.jmb.2005.01.064
Accession: 011752532
The proposed kinetic folding mechanism of the alpha-subunit of tryptophan Western synthase (alpha TS), a TIM barrel protein, displays multiple unfolded and intermediate forms which fold through four parallel pathways to reach the native state. To obtain insight into the secondary structure that stabilizes a set of late, highly populated kinetic intermediates, the refolding of urea-denatured alpha TS. from Escherichia coli was monitored by pulse-quench hydrogen exchange mass spectrometry.

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Related References

Wintrode, P.L.; Rojsajjakul, T.; Vadrevu, R. 2005: An Obligatory Intermediate Controls the Folding of the a-Subunit of Tryptophan Synthase, a TIM Barrel Protein Journal of Molecular Biology 347(5): 1-19
Wu, Y.; Vadrevu, R.; Yang, X.; Matthews, C.R. 2005: Specific structure appears at the N terminus in the sub-millisecond folding intermediate of the alpha subunit of tryptophan synthase, a TIM barrel protein Journal of Molecular Biology 351(3): 445-452
Wu, Y.; Vadrevu, R.; Kathuria, S.; Yang, X.; Matthews, C.R. 2007: A tightly packed hydrophobic cluster directs the formation of an off-pathway sub-millisecond folding intermediate in the alpha subunit of tryptophan synthase, a TIM barrel protein Journal of Molecular Biology 366(5): 1624-1638
Bilsel, O.; Zitzewitz, J.A.; Bowers, K.E.; Matthews, C.R. 1999: Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels Biochemistry 38(3): 1018-1029
Vadrevu, R.; Falzone, C.J.; Matthews, C.R.bert 2000: NMR assignments and protein folding studies of the alpha subunit of tryptophan synthase, a 8 barrel protein Biophysical Journal 78(1 Part 2): 422A
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Zitzewitz, J.A.; Matthews, C.R. 1999: Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein Biochemistry 38(31): 10205-10214
Bilsel, O.; Zitzewitz, J.A.; Bowers, K.E. 1999: Folding mechanism of the a-subunit of tryptophan synthase, an a/b barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels Biochemistry (American Chemical Society) 38(3): 18-29
Vadrevu, R.; Wu, Y.; Matthews, C.R. 2008: NMR analysis of partially folded states and persistent structure in the alpha subunit of tryptophan synthase: implications for the equilibrium folding mechanism of a 29-kDa TIM barrel protein Journal of Molecular Biology 377(1): 294-306
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Beasty, A.M.; Matthews, C.R. 1985: Characterization of an early intermediate in the folding of the alpha subunit of tryptophan synthase by hydrogen exchange measurement Biochemistry 24(14): 3547-3553
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