Section 12
Chapter 11,753

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


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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