NDLI: Folding subdomains of thioredoxin characterized by native-state hydrogen exchange.

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Folding subdomains of thioredoxin characterized by native-state hydrogen exchange.

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Folding subdomains of thioredoxin characterized by native-state hydrogen exchange.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Udgaonkar, Jayant B. Bhutani, Nidhi
Description	Country affiliation: India Author Affiliation: Bhutani N ( National Centre for Biological Sciences, Tata Institute of Fundamental Research, University of Agricultural Sciences at the Gandhi Krishi Vigyan Kendra Campus, Bangalore 560065, India.)
Abstract	Native-state hydrogen exchange (HX) studies, used in conjunction with NMR spectroscopy, have been carried out on Escherichia coli thioredoxin (Trx) for characterizing two folding subdomains of the protein. The backbone amide protons of only the slowest-exchanging 24 amino acid residues, of a total of 108 amino acid residues, could be followed at pH 7. The free energy of the opening event that results in an amide hydrogen exchanging with solvent (DeltaG(op)) was determined at each of the 24 amide hydrogen sites. The values of DeltaG(op) for the amide hydrogens belonging to residues in the helices alpha(1), alpha(2), and alpha(4) are consistent with them exchanging with the solvent only when the fully unfolded state is sampled transiently under native conditions. The denaturant-dependences of the values of DeltaG(op) provide very little evidence that the protein samples partially unfolded forms, lower in energy than the unfolded state. The amide hydrogens belonging to the residues in the beta strands, which form the core of the protein, appear to have higher values of DeltaG(op) than amide hydrogens belonging to residues in the helices, suggesting that they might be more stable to exchange. This apparently higher stability to HX of the beta strands might be either because they exchange out their amide hydrogens in a high energy intermediate preceding the globally unfolded state, or, more likely, because they form residual structure in the globally unfolded state. In either case, the central beta strands-beta(3,) beta(2), and beta(4)-would appear to form a cooperatively folding subunit of the protein. The native-state HX methodology has made it possible to characterize the free energy landscape that Trx can sample under equilibrium native conditions.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	8
Volume Number	12
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2003-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Hydrogen Metabolism Protein Folding Thioredoxins Chemistry Amides Deuterium Exchange Measurement Escherichia Coli Proteins Guanidine Pharmacology Hydrogen-ion Concentration Kinetics Magnetic Resonance Spectroscopy Models, Molecular Protein Denaturation Drug Effects Protein Structure, Secondary Protein Structure, Tertiary Protons Thermodynamics Research Support, Non-u.s. Gov't Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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