Apparent local stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: Implications for redox potential regulation and flavodoxin folding
Protein Sci STEENSMA et al.
7: 306
Data Supplement
Files in this Data Supplement:
Steensma.txt
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Description of supplementary materials.
Table1.doc
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A Microsoft Word 5.0 for Macintosh file. It contains the chemical shifts of the 1H, 15N, and 13C backbone and the 1Hbeta and 13Cbeta resonances of A. vinelandii holoflavodoxin II in 90% H2O/10% D2O, 150 mM potassium pyrophosphate, pH 6.0, 303K.
Table2.doc
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A Microsoft Word 5.0 for Macintosh file. It gives the logarithm of the amide proton exchange rates and the calculated apparent free energies (298K) for A. vinelandii holoflavodoxin II in 150 mM potassium pyrophosphate, pH 6.2, 303K.
