Multi-state unfolding of the alpha subunit of tryptophan synthase, a TIM barrel protein: Insights into the secondary structure of the stable equilibrium intermediates by hydrogen exchange mass spectrometry

Journal of Molecular Biology

Volumn 341, Issue 1, 2004, Pages 241-253

  Rojsajjakul, Teerapat ^a   Wintrode, Patrick ^a   Vadrevu, Ramakrishna ^b   Robert Matthews, C ^b   Smith, David L ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

^b UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

CD, circular dichroism; hydrogen exchange; mass spectrometry; protein folding; TIM barrel; tryptophan synthase; TS, subunit of tryptophan synthase from Escherichia coli

Indexed keywords

ACID; AMIDE; DEUTERIUM; HYDROGEN; PROTEIN SUBUNIT; TRYPTOPHAN SYNTHASE; UREA;

ARTICLE; ATOM; CIRCULAR DICHROISM; ENZYME STRUCTURE; ESCHERICHIA COLI; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTON TRANSPORT; SAMPLING; ULTRAVIOLET RADIATION;

ESCHERICHIA COLI;

EID: 4143057003     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.05.062     Document Type: Article

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