| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10870970 | FEBS Letters | 2013 | 7 Pages |
Abstract
⺠The inactive four variants can suppress aggregation and improve the activation yield during AK refolding. ⺠The more efficiency of Q63A in chaperoning AK folding may associate with its more solvent-exposed global structures. ⺠Surface hydrophobicity and hydrophobic active pocket of rhCyPA are two key factors for chaperoning AK folding. ⺠Another protein is shown to be chaperoned by CyPA, which is essential to understand the general roles of CyPA in the cell.
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Authors
Xin-Chao Zhang, Wei-Dong Wang, Jin-Song Wang, Ji-Cheng Pan,