| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10537176 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2013 | 10 Pages |
Abstract
⺠The C-terminal domain may use its Iâ²-helix to adjust N-terminal domain structure. ⺠Iâ²-helix variants of intact KatG had increasingly reduced stability and activity. ⺠Multiple substitutions gave properties of the stand-alone N-terminal domain (KatGN). ⺠Iâ²-helix variants of KatGC had diminished capacity to reactivate KatGN. ⺠KatGN reactivation by KatGC is valuable for exploring KatG structure and function.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Yu Wang, Douglas C. Goodwin,